Relevant bibliographies by topics / Isoenzymes

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Isoenzymes'

Author: Grafiati
Published: 4 June 2021
Last updated: 30 July 2024

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Journal articles on the topic "Isoenzymes"

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Sharma, R. K., and J. Kalra. "Characterization of calmodulin-dependent cyclic nucleotide phosphodiesterase isoenzymes." Biochemical Journal 299, no. 1 (April 1, 1994): 97–100. http://dx.doi.org/10.1042/bj2990097.

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Calmodulin-dependent phosphodiesterase (CaMPDE) is one of the key enzymes involved in the complex interactions which occur between the cyclic-nucleotide and Ca2+ second-messenger systems. Calmodulin-dependent phosphodiesterase exists in different isoenzymic forms, which exhibit distinct molecular and/or catalytic properties. The kinetic properties suggest that the 63 kDa brain isoenzyme is distinct from the brain 60 kDa and heart and lung CaMPDE isoenzymes. The CaMPDE isoenzymes of 60 kDa from brain, heart and lung are regulated by calmodulin, but the affinities for calmodulin are different. At identical concentrations of calmodulin, the bovine heart CaMPDE isoenzyme is stimulated at a much lower Ca2+ concentration than the bovine brain or lung isoenzymes. The bovine lung CaMPDE isoenzyme contains calmodulin as a tightly bound subunit, so that a change in calmodulin concentration had no effect on the [Ca2+]-dependence of activation of this isoenzyme. These observations are consistent with the notion that differential regulation by calmodulin and Ca2+ is an important function of these isoenzymes, which provide fine-tuning mechanisms for calmodulin action.
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Parviainen, M. T., J. H. Galloway, J. H. Towers, and J. A. Kanis. "Alkaline phosphatase isoenzymes in serum determined by high-performance anion-exchange liquid chromatography with detection by enzyme reaction." Clinical Chemistry 34, no. 12 (December 1, 1988): 2406–9. http://dx.doi.org/10.1093/clinchem/34.12.2406.

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Abstract This rapid, reproducible method for separating and determining individual alkaline phosphatase (EC 3.1.3.1) isoenzymes in serum is based on high-performance liquid chromatography with a weak anion-exchange column (SynChropak AX 300). The isoenzymes so resolved are detected by using an on-line enzyme reaction followed by spectrophotometric monitoring at 405 nm of the 4-nitrophenol formed. Complete diagnostic profiles of the various isoenzymes present in normal and pathological sera are obtained within 20 min. The mean (and SD) normal concentrations of the bone B1 and intestinal isoenzymes in serum of adults were 3.7 (4.3) and 4.5 (3.9) U/L, respectively (n = 14), and of the bone isoenzyme B2 and liver isoenzymes L1 and L2, 5.8 (8.6), 33.0 (10.6), and 12.0 (4.8) U/L, respectively (n = 17). Concentrations of the B2 and L1 isoenzymes in adults over age 40 years differed significantly from those in adults younger than 40 years, that of bone isoenzyme being lower (P less than 0.05) and that of the liver isoenzyme being higher (P less than 0.001) in the younger adults.
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Schreiber, W. E., and L. Whitta. "Alkaline phosphatase isoenzymes resolved by electrophoresis on lectin-containing agarose gel." Clinical Chemistry 32, no. 8 (August 1, 1986): 1570–73. http://dx.doi.org/10.1093/clinchem/32.8.1570.

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Abstract With this electrophoretic method the liver, biliary, and bone isoenzymes of alkaline phosphatase are clearly separated on agarose gels. Wheat-germ lectin, incorporated in the gel matrix, binds the bone isoenzyme selectively, forming a precipitate near the origin. Neither liver nor biliary isoenzyme is affected. Activity staining with an indigogenic dye substrate reveals the liver isoenzyme migrating nearest the anode, followed by the biliary and bone isoenzymes. Results are generally similar to those of electrophoresis on cellulose acetate. However, the lectin-agarose gels better resolve the liver and bone isoenzymes, and heat treatment of samples is not required before electrophoresis.
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Balogun, Kayode, Megan Lee, and Kelly Doyle. "Comparison of Heat Fractionation and Gel Electrophoresis Methods for the Quantitative Determination of Alkaline Phosphatase Isoenzymes." American Journal of Clinical Pathology 154, Supplement_1 (October 2020): S8. http://dx.doi.org/10.1093/ajcp/aqaa137.014.

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Abstract Introduction Alkaline phosphatase (ALP) is important in the diagnostic work-up for hepatobiliary and bone diseases. ALP isoenzymes are expressed in the bone, liver, kidney, placenta, and intestine, and vary in heat stability and electrophoretic mobility. Distinguishing the different ALP isoenzymes is clinically important for the diagnosis of pathologies associated with elevated ALP activity. Current modalities available to measure ALP isoenzymes utilize the heat stability, electrophoretic mobility, and immunochemical properties of the isoenzymes. The differences inherent in these methods allow for unique benefits of each method in identifying ALP isoenzymes. The objective of this study was to compare bone, liver, and placental ALP isoenzyme results determined by heat fractionation and gel electrophoresis and to characterize the heat-stable non-liver fraction (t1/2 >11 min), reported by heat fractionation, using gel electrophoresis. Methods A total of 72 de-identified serum samples that span a wide range of known ALP isoenzyme concentrations and disease states were used to measure ALP using gel electrophoresis and heat fractionation. Heat fractionation was achieved by selective inactivation of the isoenzymes at 56 °C in 10, 15, and 20-minute intervals. Log-percent activity of the total and heat-inactivated fractions at each time point was plotted against time in minutes. The linear activity decay between 10 and 20 minutes determined the relative amount of liver isoenzyme activity and the slope of the line determined the half-lives of ALP isoenzymes. Electrophoresis was performed according to the manufacturer’s protocol using the Hydragel ISO-PAL gel to resolve ALP isoenzymes based on their electrophoretic mobility and interaction with lectin. ALP isoenzymes were quantified by densitometry. Results Our results show a significant correlation coefficient (r) of 0.98, Deming regression slope of 1.1, and bias of -1.2% for the liver isoenzyme (n=43). However, liver fractions are not distinguishable by heat fractionation when heat-stable isoforms are present. The bone fraction (n=43) showed a coefficient of correlation of 0.86, slope of 0.55, and bias of -31%. Although, with a small sample size (n=6), the placental isoenzyme showed a significant agreement between the two methods: r = 0.999, slope = 0.98, and a -3.5% bias. Of the non-liver fractions reported by heat fractionation (n=13, ALP >100 U/L) eleven (85%) showed distinct qualitative bands in the intestinal lane on gel electrophoresis; however, quantitative values did not correlate between the two methods. Conclusion Our data support an agreement between the heat fractionation and gel electrophoresis methods for the quantitative determination of liver and placental alkaline phosphatase isoenzymes. Although there is an association between the two methods, the activity of the bone isoenzyme was underestimated by the gel electrophoresis method, likely due to saturation of the gel and densitometry scan because of elevated protein concentrations. The non-liver fractions were qualitatively identified as intestinal isoenzyme.
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Oliveira, Daria Pimenta de, Luiz Edson Mota de Oliveira, and Nelson Delú Filho. "Optimization of invertase assay conditions in rubber tree plants (Hevea brasiliensis Muell. Arg.)." Revista Árvore 30, no. 5 (October 2006): 687–92. http://dx.doi.org/10.1590/s0100-67622006000500001.

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The objective of this work was to define the optimal conditions for invertase assay, seeking to determine the ideal parameters for the different isoenzymes of leaf and bark tissues in adult rubber trees. Assays of varying pH, sucrose concentration and temperature of the reaction medium were conducted for the two investigated isoenzymes. The results pointed out the existence of two different pH related isoforms for the two analyzed tissues, with an isoenzyme being more active at pH 5,5 and the other at neutral/alkaline pH. Leaf blade isoenzymes presented similar values for substrate concentration, whereas the bark isoenzyme presented maximum values below those previously reported. The assays at different temperatures presented similar values for leaf isoenzymes, though they have differed significantly among the obtained values.
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Giannoulaki, E. E., D. L. Kalpaxis, C. Tentas, and P. Fessas. "Lactate dehydrogenase isoenzyme pattern in sera of patients with malignant diseases." Clinical Chemistry 35, no. 3 (March 1, 1989): 396–99. http://dx.doi.org/10.1093/clinchem/35.3.396.

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Abstract Total lactate dehydrogenase (LDH; EC 1.1.1.27) activity and the percentage distribution of LDH isoenzymes were determined in 127 patients with malignant diseases. A shift in the isoenzyme patterns was observed toward the M-type, with an increase in the percentage of LDH-4 and LDH-5 isoenzymes and a slight increase in total LDH activity of all patients. Serum samples from 68 of the patients contained an abnormal isoenzyme of LDH, "LDH-1 ex," that, on agarose gel electrophoresis at pH 8.6, migrated between albumin and LDH-1 isoenzyme. Chemotherapy, radiotherapy, or surgical removal of the tumor was accompanied by disappearance of this abnormal isoenzyme. The heat stability of LDH-1 ex isoenzyme appears to be similar to that of LDH-1 but greater than that of the other LDH isoenzymes. Statistical analysis of these data demonstrated a significant correlation between malignancy and the appearance of LDH-1 ex isoenzyme (P less than 0.001). In contrast, the relationship between LDH-1 ex isoenzyme and metastasis or anatomical location of the malignancy is not statistically important (P less than 0.1).
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BOWKER-KINLEY, Melissa M., I. Wilhelmina DAVIS, Pengfei WU, A. Robert HARRIS, and M. Kirill POPOV. "Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex." Biochemical Journal 329, no. 1 (January 1, 1998): 191–96. http://dx.doi.org/10.1042/bj3290191.

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Tissue distribution and kinetic parameters for the four isoenzymes of pyruvate dehydrogenase kinase (PDK1, PDK2, PDK3 and PDK4) identified thus far in mammals were analysed. It appeared that expression of these isoenzymes occurs in a tissue-specific manner. The mRNA for isoenzyme PDK1 was found almost exclusively in rat heart. The mRNA for PDK3 was most abundantly expressed in rat testis. The message for PDK2 was present in all tissues tested but the level was low in spleen and lung. The mRNA for PDK4 was predominantly expressed in skeletal muscle and heart. The specific activities of the isoenzymes varied 25-fold, from 50 nmol/min per mg for PDK2 to 1250 nmol/min per mg for PDK3. Apparent Ki values of the isoenzymes for the synthetic analogue of pyruvate, dichloroacetate, varied 40-fold, from 0.2 mM for PDK2 to 8 mM for PDK3. The isoenzymes were also different with respect to their ability to respond to NADH and NADH plus acetyl-CoA. NADH alone stimulated the activities of PDK1 and PDK2 by 20 and 30% respectively. NADH plus acetyl-CoA activated these isoenzymes nearly 200 and 300%. Under comparable conditions, isoenzyme PDK3 was almost completely unresponsive to NADH, and NADH plus acetyl-CoA caused inhibition rather than activation. Isoenzyme PDK4 was activated almost 2-fold by NADH, but NADH plus acetyl-CoA did not activate above the level seen with NADH alone. These results provide the first evidence that the unique tissue distribution and kinetic characteristics of the isoenzymes of PDK are among the major factors responsible for tissue-specific regulation of the pyruvate dehydrogenase complex activity.
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Perrey, Ralf, Marie-Theres Hauser, and Michael Wink. "Cellular and Subcellular Localization of Peroxidase Isoenzymes in Plants and Cell Suspension Cultures from Lupinus polyphyllus." Zeitschrift für Naturforschung C 44, no. 11-12 (December 1, 1989): 931–36. http://dx.doi.org/10.1515/znc-1989-11-1210.

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Abstract , leaf protoplasts and cell suspension cultures of Lupinus polyphyllus and isolated vacuoles were studied for cellular and subcellular localization of peroxidase isoenzymes. Isoelectric focusing revealed 16 peroxidase isoenzymes. The basic peroxidase isoenzymes are predominantly localized in the vacuole and, to a minor degree, unbound in the intercellular space. The acidic isoenzymes are cell wall-bound in plants and not detectable in suspension-cultured cells. Large amounts (up to 11.0 U/ml) of a single basic isoenzyme are detectable in the spent medium of cell suspension cultures.
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Bar, Jair, Stuart Spencer, Shethah Morgan, Laura Pike, David Cunningham, Jane D. Robertson, Juliane M. Jürgensmeier, and Glenwood D. Goss. "Correlation of lactate dehydrogenase (LDH) isoenzyme profile with outcome in advanced colorectal cancer (CRC) patients (pts) treated with chemotherapy and bevacizumab (BEV) or cediranib (CED)." Journal of Clinical Oncology 30, no. 15_suppl (May 20, 2012): e13541-e13541. http://dx.doi.org/10.1200/jco.2012.30.15_suppl.e13541.

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e13541 Background: There is a clinical need for predictive biomarkers of efficacy of VEGF signaling inhibitors (VSIs). LDH is a tetramer that can include any combination of the M and H subunits. LDH4 and 5 isoenzymes are composed mostly of the M subunit and are more abundant in hypoxic conditions. We speculated that the levels of LDH isoenzymes in pts serum may correlate with outcome of pts treated with VSIs. HORIZON I trial enrolled pts that were randomized to mFOLFOX6 with BEV or CED. A retrospective exploratory analysis was performed on baseline serum samples of these pts. Methods: Total serum LDH was tested on fresh samples during the conduct of the trial. About 2 years after the trial, frozen samples stored at -70 degrees were tested for total serum LDH and LDH isoenzymes, measured by agarose electrophoresis and a colorimetric enzymatic assay. Relative levels of M and H subunits were derived based on the known structure of each isoenzyme. Progression free survival (PFS) and overall survival (OS) were compared by subgroups of total LDH and LDH isoenzyme levels. P values were not calculated for these exploratory analyses. Results: Baseline total LDH levels from fresh serum were available for 207 pts. Total and isoenzyme LDH levels were available for frozen serum samples of 189 pts. Total LDH in the frozen and fresh samples correlated (R=0.9). Distant isoenzymes (e.g. LDH1 and 5) were negatively correlated. High M/H subunits ratio correlated with poor OS (HR=1.804, 95%CI 1.24-2.620). A non-significant trend for better OS to CED-treated vs. BEV-treated pts was seen in pts with high M/H ratio (e.g., CED 30mg vs BEV HR=0.685, 95%CI 0.382-1.23). Conclusions: Evaluation of LDH isoenzymes is feasible using serum samples kept frozen for 2 years. A negative correlation is seen between hypoxic-related and oxic-related isoenzymes. In CRC pts treated with a VSI, LDH isoenzyme hypoxia-associated profile correlates with poorer outcome. LDH isoenzyme profile as a possible predictive biomarker for benefit from CED vs. BEV requires further investigation.
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Yoshikuni, Keiko, Takashi Matsuda, Janka Poracova, Akemi Sakai, Keiko Shimada, Noriko Tabuchi, and Kiyoh Tanishima. "Phylogenic Study of Denaturation of Lactate Dehydrogenase Isoenzymes from Different Species by High and Low Temperature." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 38, no. 5 (September 2001): 548–53. http://dx.doi.org/10.1177/000456320103800513.

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We studied the influence of storage at different temperatures on lactate dehydrogenase (EC 1.1.1.27; LD) isoenzymes from different tissues and different species, and analysed biochemical and biophysical mechanisms of denaturation during storage. Isoenzymes obtained from tissue extracts of mammals, poultry, reptiles, amphibians and fish were shown to have their own denaturation ranges at low temperatures by post-treatment assays and transition temperature analysis. These ranges were between − 10 and − 20°C for most vertebrate LD isoenzymes. Circular dichroism analysis indicated that the denaturation of LD isoenzymes was probably caused by a change in the hydrophobic interactions in the molecule. At higher temperatures, LD-1 isoenzyme was more thermostable than LD-5 from the same animal species, except for rats, the LD-5 activity of which was more thermostable than the LD-1 activity. These findings indicate that variable effects of storage of samples and reference materials at low temperatures should be considered, and that it is necessary to establish LD isoenzyme standards for animal clinical laboratory investigations.
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Dissertations / Theses on the topic "Isoenzymes"

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Winter, Paul Christopher. "Isoenzymes of human galactosyltransferase." Thesis, Queen's University Belfast, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.356904.

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Perrin, Rachel. "Caractérisation de deux sous-familles d'isoenzymes du cytochrome p450 impliquées dans le métabolisme des xénobiotiques dans le cerveau." Nancy 1, 1991. http://www.theses.fr/1991NAN10462.

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Dalton, K. G. "Glutathione transferase isoenzymes in rat hepatocarcinogenesis." Thesis, University of Bradford, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.379829.

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Troughton, P. R. "Isoenzymes of rat glutathione S-transferase." Thesis, University of Bradford, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.371503.

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Rena, Neil Graham. "Identification and analysis of phosphodiesterase isoenzymes." Thesis, University of Glasgow, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.390767.

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Kaldis, Philipp. "Mitochondrial creatine kinase isoenzymes : structure/function-relationship /." [S.l.] : [s.n.], 1994. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=10686.

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López-Solache, Irma. "Characterization and expression of 5Ã-reductase isoenzymes." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp02/NQ43087.pdf.

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Manganaris, Athanasios Georgiou. "Isoenzymes as genetic markers in apple breeding." Thesis, Imperial College London, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.389070.

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Blain, Hubert. "Exploration in vitro et ex vivo du pouvoir inhibiteur des anti-inflammatoires non stéroi͏̈diens vis-à-vis des iso-enzymes de la cyclooxygénase." Nancy 1, 2002. http://docnum.univ-lorraine.fr/public/SCD_T_2002_0291_BLAIN.pdf.

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Gorbea, Carlos M. "Expression and glycosylation of meprin isoforms." Diss., This resource online, 1992. http://scholar.lib.vt.edu/theses/available/etd-07282008-134351/.

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Books on the topic "Isoenzymes"

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Boyce, Julian. Lactate dehydrogenase isoenzymes in malignant serous effusions. [s.l: The Author], 1989.

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International, Congress on Genes Gene Families and Isozymes (13th 2005 Shanghai China). Proceedings of the XIII International Congress on Genes, Gene Families, and Isozymes: Shanghai, China, September 17-21, 2005. Bologna: MEDIMOND, International Proceedings, 2003.

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Pereira-Lorenzo, S. Características morfológicas e isoenzimáticas de los cultivares de castaño (Castanea sativa Mill.) de Andalucía. Madrid: Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, 2003.

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Société belge de chimie clinique. International Symposium. Plasma isoenzymes: The current status : proceedings of the 3rd International Symposium of the Belgian Society of Clinical Chemistry, Brugge, October 24-26, 1985. Edited by Blaton V and Steirteghem A. Van. Basel ; New York: Karger, 1986.

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Pereira-Lorenzo, S. Características morfológicas e isoenzimáticas de los cultivares de castaño (Castanea sativa Mill.) de Andalucía. Madrid: Ministerio de Ciencia y Tecnología, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, 2003.

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Boyce, Julian. Isoenzymes as markers for malignancy in serous effusions. [s.l: The Author], 1992.

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Škrha, Jan. Clinical significance of amylase isoenzyme determination. Praha: Univerzita Karlova, 1987.

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Lenman, Marit. Studies on the structure, localization, and expression of myrosinase. Uppsala: Sveriges lantbruksuniversitet, 1992.

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Nicole, Pasteur, ed. Manuel technique de génétique par électrophorèse des protéines. Paris: Technique et documentation-Lavoisier, 1987.

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International Congress on Isozymes (5th 1986 Kos, Greece). Agriculture, physiology, and medicine: The third of three volumes constituting the proceedings of the 5th International Congress on Isozymes held in Kos, Greece, May 26-29, 1986. Edited by Markert Clement L. 1917-. New York: Liss, 1987.

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Book chapters on the topic "Isoenzymes"

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Gooch, Jan W. "Isoenzymes." In Encyclopedic Dictionary of Polymers, 902. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_14057.

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Pyne, N. J., and F. Burns. "Lung Phosphodiesterase Isoenzymes." In New Drugs in Allergy and Asthma, 35–49. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7324-6_4.

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Brendler, Charles B. "Isoenzymes in prostate cancer." In Cancer Treatment and Research, 1–18. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-2033-3_1.

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Gupta, G. S. "Isoenzymes in Energy Pathways." In Proteomics of Spermatogenesis, 669–94. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-27655-6_28.

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Wong, Shan S. "Lactate Dehydrogenase and its Isoenzymes." In Cardiac Markers, 171–90. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-4612-1806-7_11.

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Wu, Alan H. B. "Creatine Kinase, Isoenzymes, and Variants." In Cardiac Markers, 113–25. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-4612-1806-7_7.

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Mannervik, Bengt. "The Isoenzymes of Glutathione Transferase." In Advances in Enzymology - and Related Areas of Molecular Biology, 357–417. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470123034.ch5.

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Luz, C. M., R. H. Schirmer, J. Hamer, and W. Sachsenheimer. "Adenylate Kinase Isoenzymes in Intracranial Tumors." In Extra-Intracranial Vascular Anastomoses Microsurgery at the Edge of the Tentorium, 260–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70603-5_39.

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Harden, T. Kendall, Theresa M. Filtz, Andrew Paterson, Marie-Christine Galas, José L. Boyer, and Gary L. Waldo. "Regulation of Phospholipase C-β Isoenzymes." In Frontiers in Bioactive Lipids, 257–63. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5875-0_34.

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Hakvoort, T. B. M., G. J. C. Ruyter, K. M. C. Sinjorgo, and A. O. Muijsers. "Isoenzymes of Human Cytochrome c Oxidase." In Cytochrome Systems, 343–44. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_47.

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Conference papers on the topic "Isoenzymes"

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Рудакова, Анжела, Сергей Рудаков, and Юрий Чесноков. "Изучение полиморфизма эстеразных изоферментов в семенах картирующей популяции яровой мягкой пшеницы." In VIIth International Scientific Conference “Genetics, Physiology and Plant Breeding”. Institute of Genetics, Physiology and Plant Protection, Republic of Moldova, 2021. http://dx.doi.org/10.53040/gppb7.2021.44.

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Using electrophoresis, in 114 recombinant hybrid lines of the mapping population of spring bread wheat and in 2 parental forms, 7 esterase isoenzymes were found: A1-A7 (Mr 93-138 kDa). According to their esterase composition, all samples were subdivided into 17 zymotypes. Isoforms A4 and A6 are pre-sent in all zymotypes, i.e. are monomorphic. The other 5 isozymes provide a high level of polymorphism in the population. The majority of genotypes belong to the zymotype Gr. 1 (27%), which includes 6 isoforms. Among them there are isoforms A1 and A7, characteristic only for each of the parent forms, which indicates the codominant inheritance of these isoenzymes.
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Li, Jin, Zhiyong Ding, Zhengxin Wang, Christopher J. Logothetis, Gordon B. Mills, and Jeri Kim. "Abstract A105: Androgen regulation of 5α-reductase isoenzymes in prostate cancer: Implications for prostate cancer prevention." In Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Nov 7-10, 2010; Philadelphia, PA. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1940-6207.prev-10-a105.

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Moreb, Jan S., Mahmoud Mona, Lung-Ji Chang, Yu-Ling Yeh, John Amory, and Alex Goldstein. "Abstract 3762: The role of aldehyde dehydrogenase isoenzymes in cancer cell proliferation, migration and drug resistance." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3762.

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Sergeeva, Tatiana F., Albina N. Moshkova, Elena I. Erlykina, and Elena M. Khvatova. "Method of empirical dependences in estimation and prediction of activity of creatine kinase isoenzymes in cerebral ischemia." In Saratov Fall Meeting 2015, edited by Elina A. Genina, Valery V. Tuchin, Vladimir L. Derbov, Dmitry E. Postnov, Igor V. Meglinski, Kirill V. Larin, and Alexander B. Pravdin. SPIE, 2016. http://dx.doi.org/10.1117/12.2229863.

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Skopas, Vlasios, Dimitrios Papadopoulos, Nikolaos Trakas, Eleni Papaefstathiou, Charalampos Koufopoulos, Demosthenes Makris, Zoe Daniil, and Konstantinos Gourgoulianis. "Lactate dehydrogenase isoenzymes in patients with acute exacerbation of chronic obstructive pulmonary disease: An exploratory cross-sectional study." In ERS International Congress 2021 abstracts. European Respiratory Society, 2021. http://dx.doi.org/10.1183/13993003.congress-2021.pa1062.

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Lee, Y. J. "Lactete Dehydrogenease Isoenzymes (LDH) as Biomarker for Prediction of Acute Exacerbation and Mortality of Chronic Obstructive Pulmonary Disease (COPD)." In American Thoracic Society 2024 International Conference, May 17-22, 2024 - San Diego, CA. American Thoracic Society, 2024. http://dx.doi.org/10.1164/ajrccm-conference.2024.209.1_meetingabstracts.a1851.

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Gopalakrishna, Rayudu, Venkata S. Arepalli, Albert Elhiani, Jason E. Schiffman, and Usha Gundimeda. "Abstract 1609: Oxidation products of green tea polyphenols induce inactivation of PKC isoenzymes and induce cell death via modulation of selenoprotein thioredoxin reductase and quinone reductase." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1609.

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Van Haarlem, L. J. M., H. C. Hemker, B. A. M. Soute, and C. Vermeer. "GLA-CONTAINING PROTEINS FROM CALCIFIED HUMAN ATHEROSCLEROTIC PLAQUES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643747.

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Vitamin K-dependent carboxylase activity has been detected in human andbovine vessel wall. Studies comparingthe carboxylases from liver and vessel wall revealed that the enzyme systems may be regarded as isoenzymes withwidely different substrate specificities. The carboxylated product of vessel wall carboxylase has not yet been identified, but it seems plausible that it will be found amongst the Gla-containing proteins which are abundantly present in calcified atherosclerotic plaques (Gla= gammacarboxyglutamicacid, the abnormal amino acid formed by vitamin K-dependent carboxylase). Therefore we have started to characterize the protein constituents of hardened atherosclerotic plaques.The calcified areas from human aortae were solubilized in EDTA and the proteins extracted were partly purified by batch-wise adsorption onto QAE and elution with high salt. The crudeplaque-extract did not contain prothrombin, factor X or protein C. This excludes the possibility that Gla-containing coagulation factors are bound non-specifically from blood. Osteocalcin accounted for 20% of the total amount of protein-bound Gla-residues.Another Gla-containing protein waspurified from the crude plaque-extract by employing high performance liquid chromatography (HPLC). Gel filtration yielded a Gla-rich protein with anapparent Mr of 25 kD. In vitro boththe crude plaque-extract and the purified Gla-containing protein strongly inhibited the precipitation of calcium phosphate and calcium carbonate. A similar effect was not found with humanserum albumin nor with a thermallydecarboxylated plaque-extract. If also in vivo the Gla-containing proteinsproduced by vessel wall carboxylase prevent the precipitation of calcium salts remains to be investigated.
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Kupcho, Kevin R., Nathan J. Evans, Andrew L. Niles, Dan F. Lazar, and Thomas A. Kirkland. "Abstract 4237: Isoenzyme-selective HDAC activity assays." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4237.

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Gao, Peng, Yan Zhuang, and Charles D. Smith. "Abstract 838A: Characterization of sphingosine kinase isoenzyme selective inhibitors." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-838a.

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Reports on the topic "Isoenzymes"

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Angelov, Georgi, and Magdalena Szczepaniak. Isoenzyme Variation and Systematic Affinities among Four Elymus Species (Poaceae: Triticeae) with Different Genomic Constitution. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, May 2018. http://dx.doi.org/10.7546/crabs.2018.04.06.

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Ginzberg, Idit, Richard E. Veilleux, and James G. Tokuhisa. Identification and Allelic Variation of Genes Involved in the Potato Glycoalkaloid Biosynthetic Pathway. United States Department of Agriculture, August 2012. http://dx.doi.org/10.32747/2012.7593386.bard.

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Steroidal glycoalkaloids (SGAs) are secondary metabolites being part of the plant defense response. The two major SGAs in cultivated potato (Solanum tuberosum) are α-chaconine and α-solanine, which exhibit strong cellular lytic properties and inhibit acetylcholinesterase activity, and are poisonous at high concentrations for humans. As SGAs are not destroyed during cooking and frying commercial cultivars have been bred to contain low levels, and their content in tubers should not exceed 20 mg/100 g fresh weight. However, environmental factors can increase tuber SGA content above the safe level. The focus of the proposed research was to apply genomic approaches to identify candidate genes that control potato SGA content in order to develop tools for potato improvement by marker-assisted selection and/or transgenic approaches. To this end, the objectives of the proposal included identification of genes, metabolic intermediates and allelic variations in the potato SGAbiosynthetic pathway. The SGAs are biosynthesized by the sterol branch of the mevalonic acid/isoprenoid pathway. Transgenic potato plants that overexpress 3-hydroxy-3-methylglutaryl-CoA reductase 1 (HMG1) or squalene synthase 1 (SQS1), key enzymes of the mevalonic acid/isoprenoid pathway, exhibited elevated levels of solanine and chaconine as well as induced expression of genes downstream the pathway. These results suggest of coordinated regulation of isoprenoid (primary) metabolism and SGA secondary metabolism. The transgenic plants were further used to identify new SGA-related candidate genes by cDNA-AFLP approach and a novel glycosyltransferase was isolated. In addition, genes involved in phytosterol biosynthesis may have dual role and synthesize defense-related steroidal metabolites, such as SGAs, via lanosterol pathway. Potato lanosterol synthase sequence (LAS) was isolated and used to prepare transgenic plants with overexpressing and silencing constructs. Plants are currently being analyzed for SGA content. The dynamics of SGA accumulation in the various organs of a potato species with high SGA content gave insights into the general regulation of SGA abundance. Leaf SGA levels in S. chacoense were 10 to 20-fold greater than those of S. tuberosum. The leptines, SGAs with strong antifeedant properties against Colorado potato beetles, were present in all aerial tissues except for early and mid-developmental stages of above ground stolons, and accounted for the high SGA content of S. chacoense. These results indicate the presence of regulatory mechanisms in most tissues except in stolons that limit the levels of α-solanine and α-chaconine and confine leptine accumulation to the aerial tissues. The genomes of cultivated and wild potato contain a 4-member gene family coding for SQS. Three orthologs were cloned as cDNAs from S. chacoense and heterologously expressed in E. coli. Squalene accumulated in all E. coli lines transformed with each of the three gene constructs. Differential transcript abundance in various organs and amino acid sequence differences in the conserved domains of three isoenzymes indicate subfunctionalization of SQS activity and triterpene/sterol metabolism. Because S. chacoense and S. phureja differ so greatly for presence and accumulation of SGAs, we selected four candidate genes from different points along the biosynthetic pathway to determine if chcor phuspecific alleles were associated with SGA expression in a segregating interspecific diploid population. For two of the four genes (HMG2 and SGT2) F2 plants with chcalleles expressed significantly greater total SGAs compared with heterozygotes and those with phualleles. Although there are other determinants of SGA biosynthesis and composition in potato, the ability of allelic states at two genes to affect SGA levels confirms some of the above transgenic work where chcalleles at two other loci altered SGA expression in Desiree. Present results reveal new opportunities to manipulate triterpene/sterol biosynthesis in more targeted ways with the objective of altering SGA content for both human health concerns and natural pesticide content without disrupting the essential metabolism and function of the phytosterol component of the membranes and the growth regulating brassinosteroids.
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Watkins, Chris B., Susan Lurie, Amnon Lers, and Patricia L. Conklin. Involvement of Antioxidant Enzymes and Genes in the Resistance Mechanism to Postharvest Superficial Scald Development. United States Department of Agriculture, December 2004. http://dx.doi.org/10.32747/2004.7586539.bard.

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The objective of this research project was to evaluate the involvement of antioxidant enzymes and genes in the resistance mechanism to postharvest superficial scald development using two primary systems: 1. Resistant and susceptible progenies of an apple cross between a scald resistant crab apple, ‘White Angel’ and a scald susceptible cultivar, ‘Rome Beauty’; 2. Heat-treatment of ‘Granny Smith’, which is known to reduce scald development in this cultivar. In 2002 we asked for, and received (October 14), permission to revise our initial objectives. The US side decided to expand their results to include further work using commercial cultivars. Also, both sides wanted to include an emphasis on the interaction between these antioxidant enzymes and the á-farnesene pathway, with the cooperation of a third party, Dr. Bruce Whitaker, USDA-ARS, Beltsville. Background: Superficial scald is a physiological storage disorder that causes damage to the skin of apple and pear fruit. It is currently controlled by use of an antioxidant, diphenylamine (DPA), applied postharvest by drenching or dips, but concern exists about such chemical usage especially as it also involves application of fungicides. As a result, there has been increased emphasis on understanding of the underlying mechanisms involved in disorder development. Our approach was to focus on the oxidative processes that occur during scald development, and specifically on using the two model systems described above to determine if the levels of specific antioxidants and/or antioxidant enzyme activities correlated with the presence/absence of scald. It was hoped that information about the role of antioxidant-defense mechanisms would lead to identification of candidate genes for future transgenic manipulation. Major conclusions, solutions, achievements: Collectively, our results highlight the complexity of superficial scald developmental processes. Studies involving comparisons of antioxidant enzyme activities in different crab apple selection, commercial cultivars, and in response to postharvest heat and 1-methylcyclopropene (1-MCP) treatments, show no simple direct relationships with antioxidant contents and susceptibility of fruit to scald development. However, a correlative relationship was found between POX activity or isoenzyme number and scald resistance in most of the studies. This relationship, if confirmed, could be exploited in breeding for scald resistance. In addition, our investigations with key genes in the á-farnesenebiosynthetic pathway, together with antioxidant processes, are being followed up by analysis of exposed and shaded sides of fruit of cultivars that show different degrees of scald control by 1-MCP. These data may further reveal productive areas for future research that will lead to long term control of the disorder. However, given the complexity of scald development, the greatest research need is the production of transgenic fruit with down-regulated genes involved in á- farnesene biosynthesis in order to test the currently popular hypothesis for scald development.
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