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Journal articles on the topic 'Prolaminy'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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KANERVA, P., T. SONTAG-STROHM, and O. BRINCK. "Improved extraction of prolamins for gluten detection in processed foods." Agricultural and Food Science 20, no. 3 (2008): 206. http://dx.doi.org/10.2137/145960611797471525.

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A problem in gluten analysis has been inconsistent extractability of prolamins, particularly from processed foods consisting of unknown portions of prolamins from wheat, barley, and rye. This study aimed at improving the extraction of prolamins for immunological analysis, regardless of the cereal species and the production process. The prolamins were extracted with varying concentrations of ethanol, 1-propanol, and 2-propanol. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis and Western blotting were applied to study the protein composition of the extracts and the antibody recognition of the prolamin subgroups. We characterized the affinities of prolamin-specific antibodies that are used in gluten analysis against the prolamin groups that were soluble in 40% 1-propanol. The antibody R5 recognized more abundantly the medium-molecular weight groups, including polymeric proteins, and less the high-molecular weight groups than the anti-ù-gliadin antibody. In the present study, the prolamins were most efficiently extracted by 40% 1-propanol with 1% dithiothreitol at 50 °C . The prolamins were extracted from processed bread samples with efficiency similar to that from untreated meal samples.;

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Haas-Lauterbach, Sigrid, Ulrike Immer, Mareike Richter, and Peter Koehler. "Gluten Fragment Detection with a Competitive ELISA." Journal of AOAC INTERNATIONAL 95, no. 2 (2012): 377–81. http://dx.doi.org/10.5740/jaoacint.sge_haas-lauterbach.

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Abstract The second generation of a competitive ELISA for prolamin quantification based on the R5 antibody was studied for method performance and suitability to detect partially hydrolyzed prolamins in food. To be able to convert signal intensities to gluten concentrations, as required by the Codex Alimentarius Standard, a new calibrator consisting of a peptic-tryptic digest of wheat, rye, and barley prolamins was used for the first time. LOD and LOQ of the assay were 1.36 and 5.0 mg prolamin/kg food, respectively. Analysis of beer samples and a hydrolyzed wheat product showed that the assay provided significantly higher prolamin concentrations, compared to the sandwich ELISA based on the same antibody, which is only suitable for the detection of intact prolamins. Spiking experiments with defined concentrations of partially hydrolyzed prolamins gave recoveries ranging from 92 to 136%.

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Petr, J., I. Michalík, H. Tlaskalová, et al. "Extention of the spectra of plant products for the diet in coeliac disease." Czech Journal of Food Sciences 21, No. 2 (2011): 59–70. http://dx.doi.org/10.17221/3478-cjfs.

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The authors studied an extension of the sources of plant products for the diet in coeliac disease. This disease is induced by the components of glutenin proteins. In a collection of crops, they examined the contents of the total and protein nitrogen, the composition of protein fractions, the electrophoretic composition of reserve gluten and prolamine proteins, and the immunological determination of the gliadin amount using ELISA test. By immunological tests, gliadin content below 10 mg per 100 g of sample was found in the following species: amaranth (Amaranthus hypochondriacus and A. cruentus) followed by quinoa (Chenopodium quinoa), sorghum species &ndash; grain sorghum and sweet sorghum (Sorghum bicolor and S. saccharatum), millet (Panicum miliaceum), foxtail millet (Setaria italica ssp. maxima), broadrood (Digitaria sanguinalis) and buckwheat (Fagopyrum esculentum). These species can be considered as suitable for the diet in coeliac disease. Below-limit values were found in triticale (Triticosecale) and some oats varieties; this, however, will need some other tests. The analysed samples differred by the contents of crude protein and fraction structures of the protein complex. In pseudocereals amaranth, quinoa and buckwheat, the proportion of the soluble fractions of albumin and globulin was 50&ndash;65%. In grain sorghum, their proportion was 20.5%, in sweet sorghum 7.8%. In millet, foxtail millet, and broadrood, their proportion amounted to 12&ndash;13%. The proportion of prolamines was higher in sweet sorghum than in grain sorghum. Pseudocereals and millet contained 3&ndash;6% of prolamines, Italian millet 38.7%, and broadrood 23.1%, respectively. The two latter species had, however, lower contents of glutenins. In the other species studied, the contents of glutenins ranged from 12 to 22%. Electrophoretic analysis PAGE of prolamine proteins or SDS-PAGE ISTA, developed for gluten proteins, confirmed the results of immunological tests on the suitability of quinoa, grain sorghum, sweet sorghum, buckwheat, amaranth, broadrood, millet and foxtail millet for the diet in coeliac disease. These species did not contain prolamins or the content of -prolamins was negligible in the given samples. The tested species of wheat, triticale, and oats species were manifested as substandard or unhealthy for the diet. &nbsp;

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Wei, Dong, Wenlai Fan, and Yan Xu. "In Vitro Production and Identification of Angiotensin Converting Enzyme (ACE) Inhibitory Peptides Derived from Distilled Spent Grain Prolamin Isolate." Foods 8, no. 9 (2019): 390. http://dx.doi.org/10.3390/foods8090390.

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Distilled spent grain (DSG), the biggest by-product of the Chinese liquor industry, is rich in protein (167.8 g/kg DSG dry weight (DW)). Accounting for 60% of the total protein, prolamins are isolated from dried DSG (DDSG). In this study, angiotensin-converting enzyme (ACE) inhibitory peptides were screened from the prolamin hydrolysates of DDSG using two independent active-directed separations, ultrafiltration and reversed phase high performance liquid chromatography (RP-HPLC) coupled with ACE inhibitory activity evaluation. Six novel ACE inhibitory peptides, AVQ, YPQ, NQL, AYLQ, VLPVLS, and VLPSLN, were successfully identified and quantified from the active RP-HPLC fractions. AVQ and YPQ exhibited the highest activity, having the concentration inducing 50% inhibition (IC50) values for ACE of 181.0 and 220.0 μM, respectively. It was observed that VLPVLS was the most abundant peptide (16.96 mg/g DW) in prolamins. The results indicated that prolamin hydrolysates from DDSG could be served as a source of ACE inhibitory peptides.

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Pelger, Susanne. "Prolamin variation and evolution in Triticeae as recognized by monoclonal antibodies." Genome 36, no. 6 (1993): 1042–48. http://dx.doi.org/10.1139/g93-139.

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The isopropanol-soluble seed storage proteins, prolamins, were studied in 18 different genera of the tribe Triticeae by gel electrophoresis, Coomassie staining, and immunoblot assays. The monoclonal antibodies were originally raised against cultivated barley (Hordeum vulgare L.) hordein, and their reactions had been tested earlier on wild Hordeum species. The study showed that all the investigated Triticeae species produce prolamins and that structural similarities can be found throughout the tribe. The presence of the same antigenic sites in all the species indicates that the polypeptides contain well-conserved regions. They also indicate that the prolamins of the Triticeae species have a common evolutionary origin. In all the investigated species an antigenic site that is common to the B- and C-hordeins of barley was detected. Some of the reacting polypeptides also contained a site that is only present in the B-hordeins. The B-hordein specific site was found in all genera except Agropyron, Hordelymus, and Secale. This shows that although there are similarities between individual polypeptides, the composition of the various prolamin groups may vary between different genera. In the polyploid Elymus species different banding patterns were observed depending on what basic genomes were represented. The results suggest a direct correlation between the presence of a fast migrating polypeptide containing the B-hordein specific site and the presence of the H genome.Key words: Triticeae, prolamin, monoclonal antibodies, evolution, multigene family.

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Capouchová, I., J. Petr, H. Tlaskalová-Hogenová, et al. "Protein fractions of oats and possibilities of oat utilisation for patients with coeliac disease." Czech Journal of Food Sciences 22, No. 4 (2011): 151–62. http://dx.doi.org/10.17221/3419-cjfs.

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The applicability was evaluated of 16 different oats species and varieties of different provenance in the coeliac diet in view of the composition of the protein complex and immunological testing during two-year experiments (2001 and 2002). Determination was carried out of total nitrogen content (average of evaluated oats collection in 2001 was 2.21%, in 2002 2.78%), protein nitrogen content (average 2001 1.94%, 2002 2.28%), and crude protein (N&nbsp;&times;&nbsp;6.25) content (average 2001 13.80%, 2002 17.37%). The proportions of different protein fractions play a decisive role for the aims of this study because, based on the existing knowledge, coeliacally active protein components are present particularly in the prolamin fraction. The percentage of prolamins (determined by discontinual fractionation after Osborne) in the author&rsquo;s evaluated collection of oats species and varieties under the conditions of Central Bohemia reached on average 17.68% of the total protein in 2001, and 15.36% in 2002. The average percentage of albumins and globulins of the total protein reached 36.97% in 2001 and 41.04% in 2002, the average percentage of glutelins of the total proteins was 37.61% in 2001 and 34.10% in 2002, and residual was on average 7.55% in 2001 and 8.70% in 2002, respectively, of the total protein. Electrophoretic analysis of reserve (gluten) proteins (SDS-PAGE ISTA) showed in the oats collection evaluated the percentage of LMW + prolamins in the range 56&ndash;77% of the total reserve proteins in 2001, and 52&ndash;73% in 2002. The results of A-PAGE electrophoretic analysis of prolamin proteins confirmed the presence of &alpha;-prolamins, that ranged in the total content of prolamins from 50 to 88% in 2001, and from 77 to 100% in 2002, while &beta;- + &gamma;-prolamins ranged in 2001 from 11 to 49%, and in 2002 from 0 to 22%. These values do not give serious guarantees for the possible utilisation of oats in the gluten-free diet. The results of the immunological evaluation of the amount of prolamins in oats grains using ELISA showed great differences between different varieties and the experimental years. In 2001, 7 oats samples out of 13 evaluated, and in 2002 10 samples out of 12 evaluated were below the limit for the gluten-free diet (10 mg prolamins (gliadins)/100 g of sample dry matter), but the other varieties exceeded the limit, particularly in 2001, very significantly. The results obtained in the evaluated collection of species and varieties of oats revealed a great variability in the structure of the protein complex and in the immunological testing. In addition a significant effect of the year on the results of all analyses was evident. Based on our results, the use of oats in the diet for coeliac disease can be very risky for these reasons. &nbsp;

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Wu, Hsin-Kan, and Mei-Chu Chung. "Where is the prolamine located in rice endosperm?" Proceedings, annual meeting, Electron Microscopy Society of America 48, no. 3 (1990): 696–97. http://dx.doi.org/10.1017/s0424820100161035.

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In one of our earlier papers (Wu et al. 1978), we suggested that glutelin is the major composition of the round storage protein bodies although they also contain relatively more prolamine than the angular one does. Immunochemical studies of Krishnan et al. (1986) later showed the presence of glutelin in the irregularly-shaped (angular) protein bodies while the prolamines were found in the round ones. Our recent experiment using protein A-gold technique found that prolamine is mainly deposited into the angular protein bodies.Small blocks (1 mm3) of 7 DAF (days after flowering) caryopsis of Orvza perennis were fixed with 3% paraformaldehyde and 3% glutaraldehyde in 0.1M sodium phosphate, pH7.4, dehydrated in a graded ethanol series and infiltrated with Spurr’s resin. Thin sections, after gold labeling, were stained with uranyl acetate and lead citrate. Rabbit antibodies were raised against purified prolamine. Protein A-gold sol complex was prepared based on the technique of Horisberger et al. (1977).

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Krishnan, Hari B., Jerry A. White, and Steven G. Pueppke. "Immunocytochemical analysis of protein body formation in seeds of Sorghum bicolor." Canadian Journal of Botany 67, no. 10 (1989): 2850–56. http://dx.doi.org/10.1139/b89-366.

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Electrophoretic analysis of sorghum (Sorghum bicolor (L.) Moench) seed prolamines in the presence of sodium dodecyl sulfate reveals major proteins of 27 and 25 kDa and two other proteins of 18 and 12 kDa. Antibodies were raised against this prolamine fraction and used to examine the subcellular distribution of the proteins in developing sorghum seeds. Protein bodies in the starchy endosperm and subaleurone cells usually are round in cross section and contain darkly staining materials arranged in concentric rings. Protein bodies in the first two layers beneath the aleurone layer are irregular in shape and contain discrete pockets of light and dark staining inclusions. Prolamines were detected in both types of protein bodies by immunolabeling. Other oganelles, including Golgi complexes, mitochondria, and amyloplasts, were not labeled. The protein bodies, which have ribosomes attached to their surfaces, are directly connected to the rough endoplasmic reticulum. In some instances, this endoplasmic reticulum was specifically labeled with protein A – gold particles. Based on these observations, we suggest that the rough endoplasmic reticulum serves as the site of both synthesis and accumulation of sorghum prolamines.

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Oliveira, Aline P., Geyssa Ferreira Andrade, Bianca S. O. Mateó, and Juliana Naozuka. "Protein and Metalloprotein Distribution in Different Varieties of Beans (Phaseolus vulgaris L.): Effects of Cooking." International Journal of Food Science 2017 (2017): 1–8. http://dx.doi.org/10.1155/2017/5957178.

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Beans (Phaseolus vulgaris L.) are among the main sources of protein and minerals. The cooking of the grains is imperative, due to reduction of the effect of some toxic and antinutritional substances, as well as increase of protein digestibility. In this study, the effects of cooking on albumins, globulins, prolamins, and glutelins concentration and determination of Fe associated with proteins for different beans varieties and on phaseolin concentration in common and black beans were evaluated. Different extractant solutions (water, NaCl, ethanol, and NaOH) were used for extracting albumins, globulins, prolamins, and glutelins, respectively. For the phaseolin separation NaOH, HCl, and NaCl were used. The total concentration of proteins was determined by Bradford method; Cu and Fe associated with phaseolin and other proteins were obtained by graphite furnace atomic absorption spectrometry and by flame atomic absorption spectrometry, respectively. Cooking promoted a negative effect on (1) the proteins concentrations (17 (glutelin) to 95 (albumin) %) of common beans and (2) phaseolin concentration (90%) for common and black beans. Fe associated with albumin, prolamin, and glutelin was not altered. In Fe and Cu associated with phaseolin there was an increase of 20 and 37% for the common and black varieties, respectively.

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GAO, H. Y., D. X. HE, J. S. NIU, C. Y. WANG, and X. W. YANG. "The effect and molecular mechanism of powdery mildew on wheat grain prolamins." Journal of Agricultural Science 152, no. 2 (2013): 239–53. http://dx.doi.org/10.1017/s0021859612001049.

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SUMMARYA field experiment was conducted to investigate the effects of powdery mildew (Blumeria graminis f. sp. Tritici, Bgt) on wheat grain at varying levels of disease severity and at different growth stages. Methods used to determine these effects included Kjeldahl determination, unidimensional polyacrylamide gel electrophoresis, dielectrophoresis combined with mass spectrometric analysis. The specific influences explored were those on prolamins and protein composition at the molecular level. Concentrations of both grain protein and prolamin in wheat increased as disease indices (DIs) of powdery mildew rose from 20 days after anthesis (DAA) to maturity. Globulin concentrations changed dynamically and significantly, especially at 25 DAA when DI was the highest. This was verified by proteomic analysis which showed globulins (such as globulin 3, globulin 3B, globulin 3C, gliadin/avenin-like protein and triticin) being up-regulated significantly under powdery mildew stress. It was proposed that powdery mildew might indirectly affect protein accumulation in grain by influencing the regulative enzymes (including peptidylprolyl isomerase, cyclophilin A-2 and GTPase ObgE) and metabolic processes. It was speculated that the indirect increase caused by yield reduction was not the only factor causing the increase in prolamin concentration. Another factor may be the rise of expression level of molecular chaperones and enzymes relating to protein synthesis, which led to the rise in protein synthesis.

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Guillaumie, Sabine, Gilles Charmet, Laurent Linossier, Valérie Torney, Nathalie Robert, and Catherine Ravel. "Colocation between a gene encoding the bZip factor SPA and an eQTL for a high-molecular-weight glutenin subunit in wheat (Triticum aestivum)." Genome 47, no. 4 (2004): 705–13. http://dx.doi.org/10.1139/g04-031.

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The quality of wheat grain is largely determined by the quantity and composition of storage proteins (prolamins) and depends on mechanisms underlying the regulation of expression of prolamin genes. The endosperm-specific wheat basic region leucine zipper (bZIP) factor storage protein activator (SPA) is a positive regulator that binds to the promoter of a prolamin gene. The aim of this study was to map SPA (the gene encoding bZIP factor SPA) and genomic regions associated with quantitative variations of storage protein fractions using F7 recombinant inbred lines (RILs) derived from a cross between Triticum aestivum 'Renan' and T. aestivum 'Récital'. SPA was mapped through RFLP using a cDNA probe and a specific single nucleotide polymorphism (SNP) marker. Storage protein fractions in the parents and RILs were quantified using capillary electrophoresis. Quantitative trait loci (QTLs) for protein were detected and mapped on six chromosome regions. One QTL, located on the long arm of chromosome 1B, explained 70% of the variation in quantity of the x subunit of Glu-B1. Genetic mapping suggested that SPA is located on chromosome arm 1L and is also present in the confidence interval of the corresponding QTL for Glu-B1x on 1BL, suggesting that SPA might be a candidate gene for this QTL.Key words: Triticum aestivum, quantitative trait locus (QTL), single nucleotide polymorphism (SNP), storage protein activator (SPA), high-molecular-weight glutenin subunit (HMW-GS).

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Giovannini, Claudio, Roberto Luchetti, Elena Mancini, and Massimo de Vincenzi. "Effects of Cereal Prolamin Peptides on Differentiated CaCo-2 Cells." Alternatives to Laboratory Animals 24, no. 4 (1996): 547–52. http://dx.doi.org/10.1177/026119299602400414.

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The effects of peptic-tiyptic (PT) digests of prolamins derived from several cereals on differentiated CaCo-2 cells were studied on the nineteenth day of culture. Cell viability was determined by using the MTT assay and the colony-forming ability method. The metabolic consequences of peptide exposure were evaluated by measuring RNA, protein and glycoprotein synthesis. While PT digests from bovine serum albumin and durum wheat did not exert any effects, those derived from bread wheat, barley, rye and oats caused a dramatic inhibitory effect on metabolic synthesis and, when measured by using the colony-forming technique, a decrease in cell viability. The MTT assay did not indicate any changes in cell viability. These observations support the hypothesis that, although prolamin-derived peptides from these cereals do not exert an immediate cytotoxic effect, they are responsible for cell damage by impairment of metabolic processes.

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Ramos, Márcio Viana, Liezelotte Rezende Bomfim, Bandeira, and Henri Debray. "Evidence of an endogenous lectin receptor in seeds of the legume Cratylia floribunda." Brazilian Journal of Plant Physiology 14, no. 3 (2002): 195–202. http://dx.doi.org/10.1590/s1677-04202002000300003.

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Cratylia floribunda seeds were ground and the clean crude saline extract was fractionated into albumin, globulin, prolamin, acidic and basic glutelin protein fractions. These protein fractions were examined for the presence of an endogenous lectin receptor by SDS-polyacrylamide gel electrophoresis, western blot, affinity chromatography on a Sepharose 4B-Cratylia floribunda (CFL) lectin column and kinetic analysis in real time by surface plasmon resonance (SPR). Prolamin was the richest protein fraction although very poor in haemagglutinating activity. Basic glutelin was far the less interesting fraction for lectin activity and protein content, even though this fraction contains considerable amounts of carbohydrates. Lectin was present in all protein fractions as estimated by haemagglutinating assays but basic glutelins were almost devoid of lectin activity. Except for prolamins, protein bands were detected by SDS-PAGE in all other fractions. Western blot using digoxigenin labelled Con A revealed a single band in the albumin, globulin, acidic and basic glutelin fractions, which specifically interacted with ConA. This band migrated exactly at the same position in such fractions and seemed to be more important in the globulins. Affinity chromatography of the protein fractions on a Sepharose-CFL column yielded a peak, which was only recovered after elution with acidic buffered solution or with an alpha-D-mannose solution and the monosaccharide was recognized by the lectin. These results were fully corroborated by real time interaction of immobilized CFL with the different soluble protein fractions suggesting the presence of a lectin receptor within albumins, globulins and basic glutelins. As a whole, the results suggest that the lectin from Cratylia floribunda recognizes a soluble endogenous glycosylated receptor through an interaction mediated by its carbohydrate-binding site.

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Takaiwa, Fumio, Lijun Yang, Yuhya Wakasa, and Kenjiro Ozawa. "Compensatory rebalancing of rice prolamins by production of recombinant prolamin/bioactive peptide fusion proteins within ER-derived protein bodies." Plant Cell Reports 37, no. 2 (2017): 209–23. http://dx.doi.org/10.1007/s00299-017-2220-2.

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Kumar, Lalan, Dinesh Pandey та Anil Kumar. "Isolation, characterization and expression analysis of a nutritionally enhanced α-prolamin gene and protein during developing spikes of finger millet (Eleusine coracana)". Seed Science Research 27, № 4 (2017): 262–72. http://dx.doi.org/10.1017/s096025851700023x.

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AbstractIn the present study a combination of BLAST mediated homology search and 3′ RACE was utilized to isolate the full-length gene of Eleusine coracana alpha prolamin (Ec-α-prolamin) from finger millet. Phylogenetic analysis of Ec-α-prolamin along with related prolamin genes of different cereals and millets shows the clustering of Ec-α-prolamin in a separate group. Secondary structure prediction reveals 59.4% alpha helix structure, a structural hallmark of Ec-α-prolamin. Besides this, the protein also possesses a balanced proportion of all essential amino acids. Expression analysis based on qPCR shows increased accumulation of α-prolamin transcripts in developing grains of finger millet until attainment of seed maturity. Western blotting, using a monospecific anti-α-prolamin antibody, further confirmed the expression of a 22 kDa band in the S3 and S4 stages of developing spikes. The heterologous expression of isolated full-length Ec-α-prolamin could be potentially harnessed for making nutritionally enhanced functional food products and value-added industrial products.

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Song, Xin Xin, Xian Ming Zhao, Ya Nan Li, et al. "Isolation and Characterization of Rice Prolamin." Advanced Materials Research 365 (October 2011): 187–93. http://dx.doi.org/10.4028/www.scientific.net/amr.365.187.

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Rice prolamin, constituting 10, 13 and 16 kDa polypeptides, is indigestible and may work as a kind of ‘resistant protein’. To investigate the effective method for isolation of prolamin, in this study, prolamin fractions were extracted from defatted rice flour by 70% ethanol, 55% and 60% n-propanol, 55%, 60% and 100% ethylene glycol, and 60% isopropanol, respectively. The isolated prolamin fractions were compared and characterized by yield, efficiency of extraction and SDS-PAGE patterns. Our results indicated that the optimum extraction condition for isolation of prolamin was 55% n-propanol, with 13 kDa and 16 kDa as the dominant fractions in prolamin.

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Esen, Asim, and Khidir W. Hilu. "Prolamin and immunological studies in the Poaceae. IV. Subfamily Panicoideae." Canadian Journal of Botany 71, no. 2 (1993): 315–22. http://dx.doi.org/10.1139/b93-033.

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Representative species of 31 genera belonging to the tribes Paniceae, Andropogoneae, and Arundinelleae of the Panicoideae (Poaceae) were examined for prolamin size variation and immunological relationships to provide some insight into the systematics and evolution of the subfamily. Prolamin polypeptides were resolved by sodium dodecyl sulphate – polyacrylamide gel electrophoresis and the immunological cross-reactivities were measured by ELISA and immunoblotting. The data were analyzed both phenetically and phylogenetically. The Panicoideae contained prolamin polypeptides that ranged in size from about 10 to 35 kDa. Although no definite tribe-specific prolamin patterns were observed, genus-specific polypeptide profiles were evident. The immunological data support the monophyletic origin of the subfamily and its tribes and underscore the ancestral position of the Arundinelleae. Chionachne, subtribe Chionachninae, occupied a position distant from the subfamily that is in agreement with previous studies. The implication of these molecular data on the systematics of the subtribes is discussed. Key words: Poaceae, Panicoideae, protein, prolamin, immunology, systematics, evolution.

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Gulewicz, Krzysztof, Tadeusz Aniszewska, Wojciech Wysocki, Radosław Pilarski, and Danuta Ciesiołka. "Evaluation of the effect of various nitrogen forms on the Lupinus albus seed protein composition." Acta Societatis Botanicorum Poloniae 77, no. 2 (2011): 93–98. http://dx.doi.org/10.5586/asbp.2008.012.

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The influence of different nitrogen forms: (N2), [N2+(NH4++NO3-)], (NH4+), (NO3-), (NH4++NO3-) and (-NH2) on changes of albumin, globulin, prolamin-glutelin, non-fractioned nitrogen and non-protein nitrogen fractions of the protein seed of alkaloid-low content Lupinus albus L. cv. Butan has been studied. The experiments were performed in a greenhouse on perlite using in all cases the constant P, K, Mg and micronutrients (B, Zn, Mn, Cu, Mo, Fe) fertilization. The control was the treatment without any nitrogen support (Nd). It was clearly shown that nitrogen form has significant effect not only on the seed yield and seed protein content, but also on the composition of protein fractions and on the biological value of lupin protein. The main protein fraction of the seeds from all treatments were albumins (16.73-26.10 mgN/g). Among all the treatments, the highest level of globulin was observed for the seeds of plant growing with the symbiotic nitrogen form (15.26 mgN/g), while the lowest one for the control (Nd) (6.86 mgN/g). Symbiotic nitrogen (N2) treatment clearly increased the glutelin-prolamin fraction while the addition of mineral nitrogen (NH4++NO3-) decreased this fraction from 8.40 to 4.48 mgN/g. The lowest level of the glutelin-prolamin fraction was in the absence of any nitrogen (Nd). Non-protein fraction (Nnp) was highest in the case of plants treated with (-NH2) (9.92 mgN/g), and the lowest in the absence of nitrogen (Nd) (4.90 mgN/g). The level of non-fractioned nitrogen (Nr), with exception of [N2+(NH4++NO3-)] and -NH2 treatments, was closest to the start material. The protein fractions (albumins, globulins and glutelins and prolamins) were also electrophoretically characterized. These analysis confirmed the changes in protein composition of particular fractions under the effect of various nitrogen forms used as a fertilizer.

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Vyhnánek, T., and J. Bednář. "Polymorphism of prolamin proteins of the grain of triticale varieties certifiedin the Czech Republic." Plant, Soil and Environment 51, No. 4 (2011): 151–55. http://dx.doi.org/10.17221/3568-pse.

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&nbsp;Genetic diversity was detected in 11 varieties of triticale registered in the Czech Republic by means of polymorphism of prolamin proteins using the PAGE ISTA method. The polymorphism of prolamin proteins allowed the differentiation of the individual triticale varieties in 2002 and 2003 harvests. On the basis of Dice&rsquo;s calculations of coefficients of similarity we discovered, in parallel with the uniform genotypes, genotypes with sister prolamin spectrums with a&nbsp;different percentage of participation in the respective years. A uniform spectrum was detected in the following varieties: Disco, Kolor, Lamberto, Marko, Presto, Sekundo, Ticino and Tricolor; Kitaro and Modus were dimorphous varieties. In 2003 three sister prolamin lines appeared in the variety Gabo and in 2004 only two. In 2003 a 5% admixture of a foreign genotype was detected in the variety Marko. Typical of the unknown genotype was the gliadin block Gld&nbsp;1B3, which is the marker of rye translocation T1BL.1RS, gene Sr31 with resistance to black rust, higher cold resistance and lower baking quality of the wheat. The prolamin proteins of triticale grain are suitable for the detection of the genetic diversity and for the assessment of varietal authenticity and purity in seed samples of triticale varieties registered in the Czech Republic.

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Vyhnánek, T., J. Bednář, S. Helánová, L. Nedomová, and J. Milotová. "Use of Prolamin Polymorphism to Describe Genetic Variation in a Collection of Barley Genetic Resources." Czech Journal of Genetics and Plant Breeding 39, No. 2 (2011): 45–50. http://dx.doi.org/10.17221/3720-cjgpb.

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&nbsp;The polymorphism of prolamin storage proteins was studied in seed samples of 20 historical cultivars of&nbsp; &nbsp;spring barley (Hordeum vulgare L.) of Czech and Slovak origin, using polyacrylamide gel electrophoresis (PAGE). Only two samples were uniform. Most heterogeneity of prolamin patterns was observed in the oldest accessions. By means of a prolamin identity index it was possible to distinguish sister lines from admixtures within the seed samples. The obtained spectra will be used as additional descriptors for the spring barley core collection of the Collection of Genetic Resources of the Agricultural Research Institute Kroměř&iacute;ž, Ltd. &nbsp;

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Lyubimova, Anna, and Dmitry Eremin. "Laboratory varietal control as a guarantee of successful work of agribusiness in Russia." MATEC Web of Conferences 170 (2018): 04015. http://dx.doi.org/10.1051/matecconf/201817004015.

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A new direction of agribusiness has been formed in the modern agricultural industry. This is expressed in the appearance of highly specialized enterprises working in the field of production of high-quality seeds of agricultural crops. The use of electrophoresis method in varietal identification is a new technology in domestic agribusiness. The purpose of the research was to study the electrophoresis role of prolamins in varietal identification of crops for high-quality seed material. The laboratory of varietal identification of seeds analyzed 47 varieties of oats Russian selection. On the basis of data on the component composition of avenin, varieties with a high level of intersort genetic differences were identified: Megion, Fobos, Local (K-8427), Uspekh, Otrada, Pushkinskij. Groups of samples with identical component composition of prolamins were found. Their genetic formulas of avenin have the following form: Avn A2B4C2, Avn A4B4C2, Avn A2B4C1 or Avn A2B1C3. It is established that the method of electrophoresis of oat prolamins allows effectively distinguish varieties belonging to the same variety and indistinguishable by morphological features. Implementation of a system of regular laboratory control of purity and compliance of original and reproductive oats seeds by electrophoresis of prolamins is necessary to improve the competitiveness of Russian grain production in the world market.

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HULÍN, Petr, Pavel DOSTÁLEK, and Igor HOCHEL. "Determination of Barley Prolamins in Beer and Brewing Materials." Kvasny Prumysl 53, no. 9 (2007): 273–76. http://dx.doi.org/10.18832/kp2007015.

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Polišenská, I., L. Nedomová, and T. Vyhnánek. "Characterisation of oat genetic resources using electrophoresis of avenins." Czech Journal of Genetics and Plant Breeding 47, No. 4 (2011): 166–71. http://dx.doi.org/10.17221/42/2011-cjgpb.

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The prolamin (avenin) patterns of&nbsp; oat (Avena sativa L.) cultivars released in&nbsp; the Czech Republic and in the former Czechoslovak Republic were analysed&nbsp; by acid polyacrylamide gel electrophoresis (A-PAGE).&nbsp; Forty-nine oat (Avena sativa L.) accessions of domestic origin, maintained in the Czech collection of oat genetic resources, were analysed. The evaluated set contained 18 modern&nbsp; and 31 old cultivars. Thirty accessions showed a homogeneous prolamin pattern. The other accessions were heterogeneous with two or three different patterns, present at different percentages. Heterogeneity was present in 48% of the old cultivars, but&nbsp; only in 22% of the modern cultivars. Identity indexes within the heterogeneous accessions were calculated. The index values ranged from 0.09 to 0.75. Only in two heterogeneous cultivars (Dětenick&yacute; B&iacute;l&yacute;, Valečovsk&yacute; B&iacute;l&yacute;) the identity index between their components was higher than 0.6, indicating, that their components were most likely sister lines. All analysed cultivars could be unambiguously distinguished by their prolamin pattern. The obtained prolamin patterns will be used to complete descriptor data of the genetic resources&nbsp; and might be useful also in oat breeding and research.&nbsp;

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Marcellino, Lucilia, Carlos Junior, and Eugen Gander. "Characterization of Pearl Millet Prolamins." Protein & Peptide Letters 9, no. 3 (2002): 237–44. http://dx.doi.org/10.2174/0929866023408724.

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Hilu, K. W., and A. Esen. "Prolamins in systematics ofPoaceae subfam.Arundinoideae." Plant Systematics and Evolution 173, no. 1-2 (1990): 57–70. http://dx.doi.org/10.1007/bf00937763.

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Suman and Pinky Boora. "Changes in Soluble Protein Fractions of Rice Varieties after Cooking by Different Methods." Indian Journal of Nutrition and Dietetics 53, no. 3 (2016): 277. http://dx.doi.org/10.21048/ijnd.2016.53.3.5298.

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The aim of this research was to study the changes in soluble protein fractions of six rice varieties cooked by four cooking methods viz. ordinary, pressure, microwave and solar cooking methods. In cooked rice albumin, globulin, prolamin and glutelin fractions ranged from 4.1 to 4.3, 11.6 to 12.2, 3.0 to 3.6 and 80.5 to 81.0 % under various cooking methods against 6.4, 14.6, 4.6 and 74.4 % in the uncooked samples. Results indicated that albumin, globulin and prolamin fractions decreased significantly after cooking. This decrease was accompanied by a significant increase in the glutelin fraction as compared to uncooked rice samples. Among cooking methods, albumin in pressure and solar, globulin in solar and prolamin in ordinary were significantly (P&lt;0.05) higher than other methods. However, in respect of glutelin content microwave and solar cooking methods were superior to ordinary but at par to pressure cooking method.

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Hamada, S. "The Transport of Prolamine RNAs to Prolamine Protein Bodies in Living Rice Endosperm Cells." PLANT CELL ONLINE 15, no. 10 (2003): 2253–64. http://dx.doi.org/10.1105/tpc.013466.

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Ellis, H. J., S. Rosen-Bronson, N. O’Reilly, and P. J. Ciclitira. "Measurement of gluten using a monoclonal antibody to a coeliac toxic peptide of A gliadin." Gut 43, no. 2 (1998): 190–95. http://dx.doi.org/10.1136/gut.43.2.190.

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Background—Future European Community regulations will require a sensitive and specific assay for measurement of coeliac toxic gluten proteins in foods marketed as gluten-free. To avoid spurious cross reactions with non-toxic proteins, specific antibodies and target antigens are required. A synthetic 19 amino acid peptide of A gliadin has been shown to cause deterioration in the morphology of small intestinal biopsy specimens of coeliac patients in remission.Aims—To develop an assay for detection of gluten in foods, based on measurement of a known toxic peptide.Methods—A monoclonal antibody raised against the toxic A gliadin peptide, with a polyclonal anti-unfractionated gliadin capture antibody, was used to develop a double sandwich enzyme linked immunosorbent assay (ELISA) for the measurement of gluten in foods.Results—Standard curves for gliadin and for rye, barley, and oat prolamins were produced. The sensitivity of the assay was 4 ng/ml of gliadin, 500 ng/ml for rye prolamins, and 1000 ng/ml for oat and barley prolamins. The assay could detect gluten in cooked foods, although at reduced sensitivity. Prolamins from coeliac non-toxic rice, maize, millet, and sorghum did not cross react in the assay. A variety of commercially available gluten- free foods were analysed; small quantities of gluten were detected in some products.Conclusion—The assay may form the basis of a sensitive method for measurement of gluten in foods for consumption by patients with coeliac disease.

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SUGIMOTO, Toshio, Kunisuke TANAKA, and Zenzaburo KASAI. "Improved extraction of rice prolamin." Agricultural and Biological Chemistry 50, no. 9 (1986): 2409–11. http://dx.doi.org/10.1271/bbb1961.50.2409.

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Sugimoto, Toshio, Kunisuke Tanaka, and Zenzaburo Kasai. "Improved Extraction of Rice Prolamin." Agricultural and Biological Chemistry 50, no. 9 (1986): 2409–11. http://dx.doi.org/10.1080/00021369.1986.10867759.

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Rumbo, Martin, Fernando Gabriel Chirdo, Carlos Alberto Fossati, and Maria Cristina Anon. "Analysis of Anti-Prolamin Monoclonal Antibody Reactivity Using Prolamin Fractions Purified by Preparative Electrophoresis." Food and Agricultural Immunology 12, no. 1 (2000): 41–52. http://dx.doi.org/10.1080/09540100099616.

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Dvořák, J., D. D. Kasarda, M. D. Dietler, et al. "Chromosomal location of seed storage protein genes in the genome of Elytrigia elongata." Canadian Journal of Genetics and Cytology 28, no. 5 (1986): 818–30. http://dx.doi.org/10.1139/g86-114.

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Additions of complete and telocentric chromosomes of Elytrigia elongata (Host) Nevski in Triticum aestivum L. 'Chinese Spring' were employed to assign the genes coding for seed storage proteins to chromosome arms in the E. elongata genome. Genes coding for prolamins equivalent to wheat gliadins were found on chromosome arms 1ES and 6Ep. Genes on chromosome arm 1ES, which is presumably the p arm, coded for several components with electrophoretic mobilities (lactate–PAGE) corresponding to those of β-, γ-, and ω- gliadins and those on chromosome arm 6Ep coded for two components with mobilities corresponding to those of β-gliadins. Amino acid sequencing of mixtures of prolamins from E. elongata and from E. pontica (Podp.) Holub, a species closely related to E. elongata, indicated that prolamins of these species correspond to α-type (which includes β-gliadins), γ-type, and ω-type gliadins. Restriction fragments of genomic DNAs from substitution lines of chromosome 6E of E. elongata in 'Chinese Spring' were separated electrophoretically in agarose gels and probed with a cloned α-type gliadin gene from 'Yamhill'. This Southern blot showed that chromosome 6E yields DNA fragments identical in size to those characteristic of the α-gliadin gene cluster that is on chromosome 6A of 'Chinese Spring', 'Cheyenne', and 'Yamhill'. These results indicate that structural genes for prolamins of Elytrigia are similar to those of wheat gliadins and are located on the same chromosome arms as those in Triticum species. A high molecular weight (HMW) protein likely to be a HMW glutenin subunit was located on the long arm of chromosome 1E, which presumably is the q arm; this also is in accordance with the location of HMW glutenin subunit genes in Triticum. It is concluded that the appearance of α-type gliadin genes on chromosomes of homoeologous group 6 in T. aestivum occurred prior to divergence of Triticum and Elytrigia but after the divergence of Secale, Hordeum, and the Triticum–Elytrigia lineages, since neither Secale or Hordeum appear to have α-type genes. It is, however, possible that α-type gliadin genes were deleted from the ancestors of Secale and Hordeum after divergence from the Triticum–Elytrigia lineage.Key words: Elytrigia elongata, gene location, prolamins, gliadins, wheat.

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Hancock, Kerrie R., Paul M. Ealing, and Derek W. R. White. "Idendification of sulphur-rich proteins which resist rumen degradation and are hydrolysed rapidly by intestinal proteases." British Journal of Nutrition 72, no. 6 (1994): 855–63. http://dx.doi.org/10.1079/bjn19940090.

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Several proteins with high proportions of S-containing essential amino acids were incubated in sheep rumen fluid in vitro and their rate of digestion was examined by sodium dodecyl sulphate-polyacrylamide-gel electrophoresis. The S-rich proteins rice prolamin (10 kDa), maize zein (10 kDa) and the 3·2 kDa pumpkin (Cucurbita maxima L.) trypsin inhibitor-1 (CMTI-1) were highly resistant to rumen fluid degradation, relative to control proteins of known degradation rate (casein, bovine serum albumin (BSA) and pea (Pisum sativum) albumin-1 (PA1)). Comparison of PA1 and a recombinant N-terminal epitope-tagged PA1 indicated that addition of the epitope caused a slight increase in resistance to rumen degradation. The proteins were also incubated with a mixture of trypsin (EC 3·4·21·4) and chymotrypsin (EC 3·4·21.1). PA1, BSA and casein were hydrolysed less rapidly than rice prolamin, maize zein and CMTI-1. Digestion by these intestinal proteases appeared to be complete. Thus, the prolamin, zein and CMTI-1 proteins are suitable candidates for expression as foreign proteins in pasture plants to increase throughput and uptake of essential amino acids in sheep.

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Yamagata, Hiroshi, Koichi Tamura, Kunisuke Tanaka, and Zenzaburo Kasai. "Cell-Free Synthesis of Rice Prolamin." Plant and Cell Physiology 27, no. 7 (1986): 1419–22. http://dx.doi.org/10.1093/oxfordjournals.pcp.a077240.

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Hilu, Khidir W., and A. Esen. "Prolamin size diversity in the Poaceae." Biochemical Systematics and Ecology 16, no. 5 (1988): 457–65. http://dx.doi.org/10.1016/0305-1978(88)90044-0.

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Vyhnánek, T., and J. Bednář. "Detection of the varietal purity in sample of harvested wheat and triticale grains by prolamin marker." Plant, Soil and Environment 49, No. 3 (2011): 95–98. http://dx.doi.org/10.17221/4096-pse.

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In 1997 and 1998 we used samples of harvested grain to verify the possibility of distinguishing 14 winter wheat genotypes and six triticale genotypes and detecting the impurity on the basis of the detection of polymorphism of prolamin kernel proteins using the methods of the PAGE ISTA. On the basis of the identity index two sister prolamin lines with different percentage of participation, which was based on the weather conditions of the year of harvest, were discovered in seven wheat genotypes (Astella, Brea, Hana, Ilona, Siria, Sofia and &Scaron;&aacute;rka) and two triticale genotypes (Torn&aacute;do and KM 779). A&nbsp;foreign genotype was detected in the Hana and Astella varieties. The identity index of the impurity to the Astella and Hana variety (i.e. ii = 0.28 and ii = 0.20, respectively) was considerably lower. In an unknown genotype (impurity) we detected the gliadin block Gld 1B3, which is the genetic marker of rye translocation T1BL.1RS, the Sr31 gene of resistance to black rust, higher cold resistance and the marker of poor baking quality (presence of secalin genes). The results proved the potential practical application of the method of electrophoretic detection of polymorphism of prolamin proteins as markers of impurities of foreign genotypes in a&nbsp;seed sample.

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Vyhnánek, Tomáš. "Polymorphism of prolamin proteins in selected varieties of winter wheat registered in the Czech Republic." Acta Universitatis Agriculturae et Silviculturae Mendelianae Brunensis 56, no. 5 (2008): 221–26. http://dx.doi.org/10.11118/actaun200856050221.

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In 2006 and 2007 samples of harvested grain were used to verify the possibility of distinguishing 12 winter wheat genotypes and of detecting impurities on the basis of polymorphism of prolamin kernel proteins. Uniform electrophoretic patterns were detected in genotypes of Athlet, Buteo, Dromos, Ebi, Etela, Florett, Livia, Simila wheat in 2006 and 2007. On the basis of the identity index two sister prolamin lines with different share, depending on the year of harvest, were discovered in 3 wheat genotypes (Astella, Brea and Hana). The proportion of sister gliadin lines in the Astella and Brea genotypes was the same in both years. There was only minor difference (± 2.5%) in the share of the sister lines in the Hana variety between the respective years, and could be influenced by environmental factors. A foreign genotype was detected in the Mona variety. The identity index of the impurity to the Mona variety (ii = 0.30) was considerably low. In the impurity the gliadin block Gld 1B3 was not detected, which is the genetic marker of rye translocation T1BL.1RS (the Sr31 gene of resistance to black rust, higher cold resistance and the marker of poor baking quality – presence of secalin genes). The results proved the potential practical application of the electrophoretic detection of polymorphism of prolamin proteins as markers of impurities of foreign genotypes in a seed sample.

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Wang, Shu-Zhen, and Asim Esen. "Expression of maize prolamins in Escherichia coli." Plant Science 42, no. 1 (1985): 49–54. http://dx.doi.org/10.1016/0168-9452(85)90027-5.

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Atienza, S. G., M. J. Giménez, A. Martín, and L. M. Martín. "Variability in monomeric prolamins in Hordeum chilense." Theoretical and Applied Genetics 101, no. 5-6 (2000): 970–76. http://dx.doi.org/10.1007/s001220051569.

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Oom, Anna, Anders Pettersson, John R. N. Taylor, and Mats Stading. "Rheological properties of kafirin and zein prolamins." Journal of Cereal Science 47, no. 1 (2008): 109–16. http://dx.doi.org/10.1016/j.jcs.2007.02.005.

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Tosi, Paola. "Trafficking and deposition of prolamins in wheat." Journal of Cereal Science 56, no. 1 (2012): 81–90. http://dx.doi.org/10.1016/j.jcs.2012.02.004.

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Parameswaran, K. Parvathy, and B. Thayumanavan. "Homologies between prolamins of different minor millets." Plant Foods for Human Nutrition 48, no. 2 (1995): 119–26. http://dx.doi.org/10.1007/bf01088307.

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HIBINO, Takashi, Kunitomo KIDZU, Takehiro MASUMURA, et al. "Amino acid composition of rice prolamin polypeptides." Agricultural and Biological Chemistry 53, no. 2 (1989): 513–18. http://dx.doi.org/10.1271/bbb1961.53.513.

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Anderson, Olin D. "The B-hordein prolamin family of barley." Genome 56, no. 3 (2013): 179–85. http://dx.doi.org/10.1139/gen-2013-0016.

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The spectrum of B-hordein prolamins and genes in the single barley cultivar Barke is described from an in silico analysis of 1452 B-hordein ESTs and available genomic DNA. Eleven unique B-hordein proteins are derived from EST contigs. Ten contigs encode apparent full-length B-hordeins and the eleventh contains a premature stop codon that will lead to a truncated B-hordein. The 11 sequences are placed within the two previously described classes, i.e., the B1- and B3-type B-hordeins. The number of ESTs assigned to each sequence is used as an estimate of relative gene transcription and expression. Three of the sequences account for 79% of the total ESTs, with one sequence comprises 32% of the total ESTs and has a variant C-terminus caused by an undefined sequence change history near the 3′ coding terminus. The 70× difference in EST distribution among sequences points to the importance of understanding differential rates of expression within closely related gene families. Analysis of available genomic sequences confirms the EST assembly and reveals one full-length and two partial sequences of pseudogenes as evidenced by no matching ESTs for the sequences and premature stop codons and frame shifts.

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Shyur, L. F., and C. S. Chen. "Nucleotide sequence of two rice prolamin cDNAs." Nucleic Acids Research 18, no. 22 (1990): 6683. http://dx.doi.org/10.1093/nar/18.22.6683.

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Hibino, Takashi, Kunitomo Kidzu, Takehiro Masumura, et al. "Amino Acid Composition of Rice Prolamin Polypeptides." Agricultural and Biological Chemistry 53, no. 2 (1989): 513–18. http://dx.doi.org/10.1080/00021369.1989.10869307.

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Chaparro Acuña, S. P., A. E. Lara Sandoval, A. Sandoval Amador, S. J. Sosa Suarique, J. J. Martínez Zambrano, and J. H. Gil González. "Caracterización funcional de la almendra de las semillas de mango [Mangifera indica L.]. (Functional Characterization of Mango Seeds Kernel [Mangifera indica L.].)." CIENCIA EN DESARROLLO 6, no. 1 (2015): 67. http://dx.doi.org/10.19053/01217488.3651.

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ResumenLa almendra de la semilla de mango fue analizada para establecer su composición química y sus propiedades funcionales, con el fin de establecer la viabilidad de su uso como ingrediente en la industria de alimentos. Se realizó el análisis proximal de la almendra de la semilla de mango (Mangifera indica L.), obtenida como desecho agroindustrial, y la caracterización funcional de la harina desengrasada. La almendra presentó la siguiente composición: proteína cruda, 6,39%, humedad, 44,8%, grasa cruda, 10,70%, cenizas, 2,4%, y fibra, 2,38%. En la harina desengrasada, la capacidad de absorción de agua y de aceite fue de 3,0 y 2,0 mL/g, respectivamente. La actividad emulsificante aumentó al incrementarse el pH, alcanzando un máximo a pH=10. Al aumentar la concentración de la dispersión harina/agua (20% p-v) se observó el incremento de la capacidad gelificante. El tipo de proteínas que contiene la harina son globulinas (40,16%), proteínas insolubles (23,84%), glutelinas (15,81%), albúminas (12,11%) y, en menor concentración, prolaminas (8,08%). La extracción de aislados proteicos se obtuvo con bajos rendimientos (menor del 2%), por lo tanto, no se cuantificaron sus propiedades funcionales. AbstractMango seeds were analyzed to establish their chemical composition and functional properties in order toinvestigate the possibility of their use as an ingredient in the food industry. The average composition of kernel was determined to be: 6,39% of crude protein, 44,8% of moisture, 10,70% of oil, 2,4% of ash and 2,38% of crude fiber. Water and oil absorption capacity of meal was 3,0 mL/g and 2,0 mL/g, respectively. Emulsifying activity increased with increasing pH peaking at 10. Increasing the concentration of the flour/water (20% bw) dispersion improved gelling ability. The type of proteins are globulins (40,16%), insoluble proteins (23,84%), glutelin (15,81%), albumin (12,11%) and less prolamin concentration (8,08%). The extraction of protein isolates, was obtained at low yields (less than 2%), therefore, their functional properties were not quantified.

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Nagy, Ila J., Imre Takács, Angéla Juhász, László Tamás, and Zoltán Bedõ. "Identification of a new class of recombinant prolamin genes in wheat." Genome 48, no. 5 (2005): 840–47. http://dx.doi.org/10.1139/g05-042.

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A novel storage protein gene with obvious wheat chimeric structure was isolated from an immature kernel-specific cDNA library prepared from the old Hungarian variety, Bánkúti 1201. This clone contains γ-gliadin sequences in the 5′ region and LMW-glutenin sequences on the 3′ end. A frameshift mutation was also introduced by the putative recombination event. Hence, the amino acid sequence of the C-terminal region was transformed to a completely new polypeptide. Based on this finding, 7 additional recombinant prolamin genes of similar structure were isolated with specific PCR primers. The 8 chimeric clones seem to be derived from 4 individual γ-gliadin and 3 LMW-glutenin sequences. These genes show remarkable diversity in size, gliadin:glutenin ratio, frameshift mutations, and sulphur content. The putative functional characteristics of the chimeric polypeptides and problems related to the origin of the encoding genes are discussed.Key words: prolamin, chimeric genes, recombination, wheat cDNA library.

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Shewry, Peter R., Gillian Hull, and Arthur S. Tatham. "Sulphur-poor prolamins of barley, wheat and rye." Biochemical Society Transactions 19, no. 2 (1991): 528–30. http://dx.doi.org/10.1042/bst0190528.

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Zhang, Wei, Vavaporn Sangtong, Joan Peterson, M. Paul Scott, and Joachim Messing. "Divergent properties of prolamins in wheat and maize." Planta 237, no. 6 (2013): 1465–73. http://dx.doi.org/10.1007/s00425-013-1857-5.

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