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Journal articles on the topic 'Arcelin'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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1

Bernal, Carolina, Daynet Sosa, Iván Galindo-Castro, and Nardy Diez. "Two-dimensional gel electrophoresis to identify arcelins from Phaseolus vulgaris with inmuno-proteomic analysis." Agronomía Colombiana 36, no. 2 (May 1, 2018): 114–19. http://dx.doi.org/10.15446/agron.colomb.v36n2.67694.

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The present study used proteomics to analyze the expression of lectin-like proteins, specifically arcelins, in P. vulgaris cultivar varieties from Venezuela. A PAGE-SDS analysis of 30 commercial accessions of P. vulgaris showed significant differences in the molecular weight range of lectin-like proteins (arcelins). Eight different accessions were selected based on their electroforetic mobility for the proteomic analysis. Arcelin immuno-detection of two dimentional electrophoresed proteins was used to easily display the different arcelin proteomic profiles of the studied accessions. Mass spectrometry analysis confirmed the arcelin nature of these proteins. This is the first report on arcelin evaluation of the Venezuelan germoplasm of P. vulgaris with the aim of enhancing breeding programs by identifying accession materials with resistance to bean storage pests.

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2

Romero Andreas, J., B. S. Yandell, and F. A. Bliss. "Bean arcelin." Theoretical and Applied Genetics 72, no. 1 (April 1986): 123–28. http://dx.doi.org/10.1007/bf00261467.

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3

Osborn, T. C., T. Blake, P. Gepts, and F. A. Bliss. "Bean arcelin." Theoretical and Applied Genetics 71, no. 6 (March 1986): 847–55. http://dx.doi.org/10.1007/bf00276428.

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4

Oriani, Maria A. de G., and Fernando M. Lara. "Oviposition preference of Bemisia tabaci (Genn.) biotype B (Homoptera: Aleyrodidae) for bean genotypes containing arcelin in the seeds." Anais da Sociedade Entomológica do Brasil 29, no. 3 (September 2000): 565–72. http://dx.doi.org/10.1590/s0301-80592000000300019.

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The oviposition preference of Bemisia tabaci biotype B (Homoptera: Aleyrodidae) for bean (Phaseolus vulgaris L.) genotypes containing arcelin in the seeds was evaluated. The tests were carried out under greenhouse conditions, in the dry and wet seasons, with the following genotypes: ARC 3s, ARC 5s (wild genotypes containing arcelin in the seeds); ARC 1, ARC 2, ARC 3, ARC 4 (near isogenic lines containing arcelin in the seeds - EMBRAPA) and Porrillo 70, Bolinha, IAPAR MD 808 (commercial genotypes without arcelin). In the free choice and no-choice oviposition tests, Bolinha and Porrillo 70 genotypes were preferred for oviposition by that insect. The Bolinha susceptibility could be related to the great number of acicular trichomes presents on its leaves surface. The wild genotypes, ARC 5s and ARC 3s, showed oviposition nonpreference resistance type. This resistance is not related to the arcelin variants, since the bred genotypes also contain arcelin in its seeds and did not show resistance to B. tabaci, biotype B.

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5

Oriani, Maria A. de G., and Fernando M. Lara. "Antibiosis effects of wild bean lines containing arcelin on Bemisia tabaci (Genn.) biotype B (Homoptera: Aleyrodidae)." Anais da Sociedade Entomológica do Brasil 29, no. 3 (September 2000): 573–82. http://dx.doi.org/10.1590/s0301-80592000000300020.

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The biology of Bemisia tabaci biotype B (Genn.) on bean (Phaseolus vulgaris L.) genotypes containing arcelin in the seeds was evaluated. Also, biochemical screening of seeds and leaves material of these genotypes were carried out in order to verify if traces of arcelin could be found in its leaves. The tests were conducted under greenhouse conditions, in the dry and wet seasons, with the following genotypes: ARC 3s, ARC 5s (wild genotypes containing arcelin in the seeds); ARC 1, ARC 2, ARC 3, ARC 4 (near isogenic lines containing arcelin in the seeds - EMBRAPA) and Porrillo 70, Bolinha, IAPAR MD 808 (commercial genotypes without arcelin). The wild genotypes, ARC 3s and ARC 5s, showed high levels of antibiosis resistance type, mainly for ARC 5s which presented the highest nymphs mortality rates, approximately 90%. Also, the longest development time for nymphs fed on ARC 5s genotype suggest antibiosis and/or feeding nonpreference resistance type. The wild genotype resistance is not related with arcelin presence in the seeds, since no trace of this protein was found in its leaves.

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6

FABRE, Christine, Henri CAUSSE, Lionel MOUREY, Jos KONINKX, Michel RIVIÈRE, Henno HENDRIKS, Germain PUZO, Jean-Pierre SAMAMA, and Pierre ROUGÉ. "Characterization and sugar-binding properties of arcelin-1, an insecticidal lectin-like protein isolated from kidney bean (Phaseolus vulgaris L. cv. RAZ-2) seeds." Biochemical Journal 329, no. 3 (February 1, 1998): 551–60. http://dx.doi.org/10.1042/bj3290551.

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Arcelin-1 is a lectin-like protein found in the seeds of wild varieties of the kidney bean (Phaseolus vulgaris). This protein displays insecticidal properties, but the mechanism of action is as yet unknown. In the present study we investigated the biochemical and biophysical properties of arcelin-1 from Phaseolus vulgaris cv. RAZ-2. Native arcelin-1 is a dimeric glycoprotein of 60 kDa, built from the non-covalent association of two identical monomers. This dimer resists dissociation by chaotropic agents and is highly resistant to proteolytic enzymes. Each subunit contains 10% (w/w) neutral sugars which belong to the high-mannose and complex-type glycans attached to three glycosylation sites. No interaction of the protein with simple sugars could be detected, but arcelin-1 displays an intrinsic specificity in binding complex glycans. Arcelin-1 therefore differs from the closely related phytohaemagglutinin lectins and α-amylase inhibitor in several respects: oligomerization states, sugar-binding affinities and the type and number of glycan chains. These features may be related to the toxicity of arcelin-1.

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7

Bliss, Fredrick A. "BREEDING STRATEGIES FOR DEVELOPING DRY BEAN CULTIVARS RESISTANT TO BRUCHID WEEVILS." HortScience 25, no. 9 (September 1990): 1123d—1123. http://dx.doi.org/10.21273/hortsci.25.9.1123d.

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The presence of arcelin protein in the seeds of common bean, Phaseolus vulgaris L., provides resistance to the Mexican bean weevil and to a lesser degree, the common bean weevil. Fast, accurate identification of single seeds containing arcelin facilitates the transfer of alleles for each of four different arcelin types through standard crossing procedures. Seed yields and other traits of near-isogenic lines that contain different alleles were comparable to the standard parent, Porrillo 70. Genotypic mixtures containing resistant and susceptible seeds produced seed yields comparable to Porrillo 70, which suggests that heterogeneous populations offer the potential for stable resistant cultivars.

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8

Lara, Fernando M. "Resistance of wild and near isogenic bean lines with arcelin variants to Zabrotes subfasciatus (Boheman): I - Winter crop." Anais da Sociedade Entomológica do Brasil 26, no. 3 (December 1997): 551–60. http://dx.doi.org/10.1590/s0301-80591997000300019.

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The objective of this study was to determine the resistance of winter crops of bean (Phaseolus vulgaris) lines with arcelin variants to Zabrotes subfasciatus (Boheman) (Coleoptera: Bruchidae). Two trials, a no-choice test and a free-choice test, were set up under laboratory conditions using genotypes Arc. 1, Arc. 2, Arc. 3 and Arc. 4 (near isogenic lines containing arcelin 1, 2, 3 and 4, respectively), genotypes Arc. 1S, Arc. 3S and Arc. 5S (wild lines containing arcelin 1, 3 and 5, respectively), and genotypes IAPAR MD-808 and Porrillo 70. Plots with 10 g of each line and a proportion of 7 adult pairs/plot were used. Attractiveness, oviposition, emergence and adult weight, mortality, developmental period, and seed weight loss were determined. Nonpreference (attraction and oviposition) was observed only for the wild genotypes Arc. 3S and Arc. 5S. The wild genotypes Arc. 5S and Arc. 1S and the near isogenic lines Arc. 1 and Arc. 2 presented high resistance of the antibiosis type to Z. subfasciatus. Arc. 4 and Arc. 3 presented moderate resistance, probably due to feeding nonpreference.

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9

Gerhardt, Isabel R., Norma S. Paes, Carlos Bloch, Paulo A. M. Mendes, Adilson Leite, Maarten J. Chrispeels, and Maria Fatima Grossi de Sa. "Molecular characterization of a new arcelin-5 gene." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1490, no. 1-2 (January 2000): 87–98. http://dx.doi.org/10.1016/s0167-4781(99)00219-5.

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10

Paes, Norma S., Isabel R. Gerhardt, Marise V. Coutinho, Massaru Yokoyama, Eliana Santana, Nicholas Harris, Maarten J. Chrispeels, and M. Fatima Grossi de Sa. "The effect of arcelin-1 on the structure of the midgut of bruchid larvae and immunolocalization of the arcelin protein." Journal of Insect Physiology 46, no. 4 (April 2000): 393–402. http://dx.doi.org/10.1016/s0022-1910(99)00122-5.

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11

Barbosa, Flávia Rabelo, Massaru Yokoyama, Pedro Antônio Arraes Pereira, and Francisco José Pfeilsticker Zimmermann. "Effect of arcelin protein on the biology of Zabrotes subfasciatus (Boheman 1833), in dry beans." Pesquisa Agropecuária Brasileira 34, no. 10 (October 1999): 1805–10. http://dx.doi.org/10.1590/s0100-204x1999001000006.

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Arcelin is a seed protein found in wild beans (Phaseolus vulgaris) which gives resistance to Mexican bean weevil, Zabrotes subfasciatus (Boheman 1833) (Coleoptera: Bruchidae). Studies were carried out with the objective of estimating the effect of four alleles of protein arcelin (Arc1, Arc2, Arc3 and Arc4) on the biology of Z. subfasciatus. The experiment was carried out in laboratory at Embrapa-Centro Nacional de Pesquisa de Arroz e Feijão, in Santo Antônio de Goiás, GO, Brazil, under non controlled conditions. The highest levels of antibiosis to Z. subfasciatus were observed in Arc1, with reduction in the number of eggs, number of emerged adults, adults longevity. In the line Arc2 only reduction in the number of emerged adults was observed. The lines Arc3 and Arc4 showed low efficiency on the reduction of progeny of Z. subfasciatus and effects in the longevity and egg-adult cycle were not detected. Insect sexual ratio was not altered by the presence of Arc1, Arc2, Arc3 and Arc4 in the seeds.

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12

Goossens, Alain, Roberto Geremia, Guy Bauw, Marc Montagu, and Geert Angenon. "Isolation and Characterisation of Arcelin-5 Proteins and cDNAs." European Journal of Biochemistry 225, no. 3 (November 1994): 787–95. http://dx.doi.org/10.1111/j.1432-1033.1994.0787b.x.

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13

OSBORNI, T. C., D. C. ALEXANDER, S. S. M. SUN, C. CARDONA, and F. A. BLISS. "Insecticidal Activity and Lectin Homology of Arcelin Seed Protein." Science 240, no. 4849 (April 8, 1988): 207–10. http://dx.doi.org/10.1126/science.240.4849.207.

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14

Fakhoury, A. M., and C. P. Woloshuk. "Inhibition of Growth of Aspergillus flavus and Fungal α-Amylases by a Lectin-Like Protein from Lablab purpureus." Molecular Plant-Microbe Interactions® 14, no. 8 (August 2001): 955–61. http://dx.doi.org/10.1094/mpmi.2001.14.8.955.

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Aspergillus flavus is a fungal pathogen of maize causing an important ear rot disease when plants are exposed to drought and heat stress. Associated with the disease is the production of aflatoxins, which are a series of structurally related mycotoxins known to be carcinogenic. Previous research has suggested that the α-amylase of A. flavus promotes aflatoxin production in the endosperm of infected maize kernels. We report here the isolation and characterization of a 36-kDa α-amylase inhibitor from Lablab purpureus (AILP). AILP inhibited the α-amylases from several fungi but had little effect on those from animal and plant sources. The protein inhibited conidial germination and hyphal growth of A. flavus. The amino acid sequence indicated that AILP is similar to lectin members of a lectin-arcelin-α-amylase inhibitor family described in common bean and shown to be a component of plant resistance to insect pests. AILP also agglutinated papain-treated red blood cells from human and rabbit. These data indicate that AILP represents a novel variant in the lectin-arcelin-α-amylase inhibitor family of proteins having lectin-like and α-amylase inhibitory activity.

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15

Bliss, F. A., J. C. Rosas, and P. A. A. Pereira. "DEPLOYMENT OF ARCELIN GENES FOR BRUCHID RESISTANCE IN COMMON BEANS." HortScience 27, no. 6 (June 1992): 597e—597. http://dx.doi.org/10.21273/hortsci.27.6.597e.

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The discovery of bruchid resistance in wild beans and the demonstration that theArcelin protein is responsible for the resistance, provide an opportunity to develop resistant cultivars of common bean, Phaseolus vulgaris L. Arcelin expression is controlled by multiple alleles, which impart different levels of insect resistance. In field tests in Honduras and Brazil, backcross-derived lines with the Arl-1 allele were most resistant, especially to Mexican bean weevil. Seed mixtures of 0.80 Arl-1:0.20 susceptible and equal amounts of Arl-1,Arl-2, and Arl-3, and Arl-4 containing seeds showed resistanc elevels and seed yields similar to lines homogeneous for Arl-1. Breeding lines uniform for appearance and agronomic performance, but heterogenous for resistance genes are being tested as potential new dry bean cultivars having stable insect resistance.

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16

Osborn, Thomas C., Mark Burow, and Fredrick A. Bliss. "Purification and Characterization of Arcelin Seed Protein from Common Bean." Plant Physiology 86, no. 2 (February 1, 1988): 399–405. http://dx.doi.org/10.1104/pp.86.2.399.

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17

John, Maliyakal E., and Christopher M. Long. "Sequence analysis of arcelin 2, a lectin-like plant protein." Gene 86, no. 2 (February 1990): 171–76. http://dx.doi.org/10.1016/0378-1119(90)90276-w.

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18

Hartweck, Lynn M., Robert D. Vogelzang, and Thomas C. Osborn. "Characterization and Comparison of Arcelin Seed Protein Variants from Common Bean." Plant Physiology 97, no. 1 (September 1, 1991): 204–11. http://dx.doi.org/10.1104/pp.97.1.204.

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19

Hamelryck, Thomas W., Freddy Poortmans, Alain Goossens, Geert Angenon, Mark Van Montagu, Lode Wyns, and Remy Loris. "Crystal Structure of Arcelin-5, a Lectin-like Defense Protein fromPhaseolus vulgaris." Journal of Biological Chemistry 271, no. 51 (December 20, 1996): 32796–802. http://dx.doi.org/10.1074/jbc.271.51.32796.

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20

Mourey, Lionel, Jean-Denis Pédelacq, Catherine Birck, Christine Fabre, Pierre Rougé, and Jean-Pierre Samama. "Crystal Structure of the Arcelin-1 Dimer fromPhaseolus vulgarisat 1.9-Å Resolution." Journal of Biological Chemistry 273, no. 21 (May 22, 1998): 12914–22. http://dx.doi.org/10.1074/jbc.273.21.12914.

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21

Foray, N. "Fabien Arcelin (1876–1942), ou comment on devient radiothérapeute quand on naît archéologue." Cancer/Radiothérapie 21, no. 3 (May 2017): 228–38. http://dx.doi.org/10.1016/j.canrad.2016.12.003.

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22

Blair, Matthew W., Claritza Muñoz, Héctor F. Buendía, José Flower, Juan M. Bueno, and César Cardona. "Genetic mapping of microsatellite markers around the arcelin bruchid resistance locus in common bean." Theoretical and Applied Genetics 121, no. 2 (April 1, 2010): 393–402. http://dx.doi.org/10.1007/s00122-010-1318-5.

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23

Suzuki, K., M. Ishimoto, M. Iwanaga, F. Kikuchi, and K. Kitamura. "Inheritance of seed α-amylase inhibitor in the common bean and genetic relationship to arcelin." Theoretical and Applied Genetics 90, no. 6 (May 1995): 762–66. http://dx.doi.org/10.1007/bf00222009.

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24

Hartweck, L. M., and T. C. Osborn. "Altering protein composition by genetically removing phaseolin from common bean seeds containing arcelin or phytohemagglutinin." Theoretical and Applied Genetics 95, no. 5-6 (October 1997): 1012–17. http://dx.doi.org/10.1007/s001220050655.

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25

Sakthivelkumar, Shanmugavel, Michael Immanuel Jesse, Velayutham Veeramani, Paulchamy Ramaraj, Krishnan Kathiravan, Munusamy Arumugam, and Sundaram Janarthanan. "Diversity and analysis of sequences encoded by arcelin genes from Indian wild pulses resistant to bruchids." Process Biochemistry 48, no. 11 (November 2013): 1697–705. http://dx.doi.org/10.1016/j.procbio.2013.08.008.

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26

Velten, Guido, Anja S. Rott, César Cardona, and Silvia Dorn. "The inhibitory effect of the natural seed storage protein arcelin on the development of Acanthoscelides obtectus." Journal of Stored Products Research 43, no. 4 (January 2007): 550–57. http://dx.doi.org/10.1016/j.jspr.2007.03.005.

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27

Anthony, Janice L., Raymond A. Vonder Haar, and Timothy C. Hall. "Nucleotide Sequence of a Genomic Clone Encoding Arcelin, a Lectin-Like Seed Protein from Phaseolus vulgaris." Plant Physiology 97, no. 2 (October 1, 1991): 839–40. http://dx.doi.org/10.1104/pp.97.2.839.

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28

N., Arumugam, Janarthanan S., Sakthivelkumar S., and Veeramani V. "Comparative Modeling and Prediction of Carbohydrate Binding Pockets in 3D Structure of Wild Pulse Lablab Purpureus Arcelin." International Journal of Computer Applications 21, no. 9 (May 31, 2011): 14–19. http://dx.doi.org/10.5120/2541-3477.

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29

Young, N. Martin, Pierre Thibault, David C. Watson, and Maarten J. Chrispeels. "Post-translational processing of two α-amylase inhibitors and an arcelin from the common bean, Phaseolus vulgaris." FEBS Letters 446, no. 1 (March 5, 1999): 203–6. http://dx.doi.org/10.1016/s0014-5793(99)00212-4.

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30

Goossens, Alain, Willy Dillen, Janniek De Clercq, Marc Van Montagu, and Geert Angenon. "The arcelin-5 Gene of Phaseolus vulgarisDirects High Seed-Specific Expression in TransgenicPhaseolus acutifolius and Arabidopsis Plants." Plant Physiology 120, no. 4 (August 1, 1999): 1095–104. http://dx.doi.org/10.1104/pp.120.4.1095.

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31

Rougé, Pierre, Annick Barre, Henri Causse, Christian Chatelain, and Gilberte Porthé. "Arcelin and α-amylase inhibitor from the seeds of common bean (Phaseolus vulgaris L.) are truncated lectins." Biochemical Systematics and Ecology 21, no. 6-7 (September 1993): 695–703. http://dx.doi.org/10.1016/0305-1978(93)90074-2.

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32

Karuppiah, Hilda, Nithya Kirubakaran, and Janarthanan Sundaram. "Genetic resources for arcelin, a stored product insect antimetabolic protein from various accessions of pulses of Leguminosae." Genetic Resources and Crop Evolution 65, no. 1 (March 28, 2017): 79–90. http://dx.doi.org/10.1007/s10722-017-0510-8.

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33

Mirkov, T. Erik, Janice M. Wahlstrom, Kiyoshi Hagiwara, Flavio Finardi-Filho, Susanne Kjemtrup, and Maarten J. Chrispeels. "Evolutionary relationships among proteins in the phytohemagglutinin-arcelin-?-amylase inhibitor family of the common bean and its relatives." Plant Molecular Biology 26, no. 4 (November 1994): 1103–13. http://dx.doi.org/10.1007/bf00040692.

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34

Duarte, Maria Angélica Gaag, Glaucia Barbosa Cabral, Abdulrazak Baba Ibrahim, and Francisco José Lima Aragão. "An overview of the APA locus and arcelin proteins and their biotechnological potential in the control of bruchids." Agri Gene 8 (June 2018): 57–62. http://dx.doi.org/10.1016/j.aggene.2018.05.001.

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35

Goossens, Alain, Constanza Quintero, Willy Dillen, Riet De Rycke, Jose Flower Valor, Janniek De Clercq, Marc Van Montagu, Cesar Cardona, and Geert Angenon. "Analysis of bruchid resistance in the wild common bean accession G02771: no evidence for insecticidal activity of arcelin 5." Journal of Experimental Botany 51, no. 348 (July 2000): 1229–36. http://dx.doi.org/10.1093/jexbot/51.348.1229.

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36

Grazziotin, Maria A. G. D., Glaucia B. Cabral, Abdulrazak B. Ibrahim, Renato B. Machado, and Francisco J. L. Aragão. "Expression of the Arcelin 1 gene from Phaseolus vulgaris L. in cowpea seeds ( Vigna unguiculata L.) confers bruchid resistance." Annals of Applied Biology 176, no. 3 (January 11, 2020): 268–74. http://dx.doi.org/10.1111/aab.12568.

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37

Goossens, Alain, Constanza Quintero, Willy Dillen, Riet De Rycke, Jose Flower Valor, Janniek De Clercq, Marc Van Montagu, Cesar Cardona, and Geert Angenon. "Analysis of bruchid resistance in the wild common bean accession G02771: no evidence for insecticidal activity of arcelin 5." Journal of Experimental Botany 51, no. 348 (July 2000): 1229–36. http://dx.doi.org/10.1093/jxb/51.348.1229.

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38

Mourey, Lionel, Jean-Denis Pédelacq, Christine Fabre, Henri Causse, Pierre Rougé, and Jean-Pierre Samama. "Small-Angle x-ray scattering and crystallographic studies of arcelin-1: An insecticidal lectin-like glycoprotein fromPhaseolus vulgaris L." Proteins: Structure, Function, and Genetics 29, no. 4 (December 1997): 433–42. http://dx.doi.org/10.1002/(sici)1097-0134(199712)29:4<433::aid-prot4>3.0.co;2-9.

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39

Cardona, Cesar, Julia Kornegay, Carmen E. Posso, Francisco Morales, and Hernando Ramirez. "Comparative value of four arcelin variants in the development of dry bean lines resistant to the Mexican bean weevil." Entomologia Experimentalis et Applicata 56, no. 2 (August 1990): 197–206. http://dx.doi.org/10.1111/j.1570-7458.1990.tb01397.x.

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40

Kolandaivel, P., P. Selvarengan, and K. V. Gunavathy. "Structure and potential energy surface studies on 310 helices of hen egg white lysozyme and Phaseolus vulgaris arcelin-1 proteins." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1764, no. 1 (January 2006): 138–45. http://dx.doi.org/10.1016/j.bbapap.2005.10.016.

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41

Minney, B. Hugo P., Angharad M. R. Gatehouse, Philip Dobie, Julie Dendy, Cesar Cardona, and John A. Gatehouse. "Biochemical bases of seed resistance to Zabrotes subfasciatus (bean weevil) in Phaseolus vulgaris (common bean); A mechanism for arcelin toxicity." Journal of Insect Physiology 36, no. 10 (January 1990): 757–67. http://dx.doi.org/10.1016/0022-1910(90)90049-l.

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42

Pusztai, A., G. Grant, J. C. Stewart, S. Bardocz, S. W. B. Ewen, and A. M. R. Gatehouse. "Nutritional evaluation of RAZ-2, a new Phaseolus vulgaris bean cultivar containing high levels of the natural insecticidal protein arcelin 1." Journal of Agricultural and Food Chemistry 41, no. 3 (March 1993): 436–40. http://dx.doi.org/10.1021/jf00027a017.

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43

Zaugg, Isabelle, Chiara Magni, Dario Panzeri, Maria Gloria Daminati, Roberto Bollini, Betty Benrey, Sven Bacher, and Francesca Sparvoli. "QUES, a new Phaseolus vulgaris genotype resistant to common bean weevils, contains the Arcelin-8 allele coding for new lectin-related variants." Theoretical and Applied Genetics 126, no. 3 (November 2, 2012): 647–61. http://dx.doi.org/10.1007/s00122-012-2008-2.

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44

Janarthanan, Sundaram, Shanmugavel Sakthivelkumar, Velayutham Veeramani, Dixit Radhika, and Subbaratnam Muthukrishanan. "A new variant of antimetabolic protein, arcelin from an Indian bean, Lablab purpureus (Linn.) and its effect on the stored product pest, Callosobruchus maculatus." Food Chemistry 135, no. 4 (December 2012): 2839–44. http://dx.doi.org/10.1016/j.foodchem.2012.06.129.

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45

Mbogo, K. P., J. Davis, and J. R. Myers. "Transfer of the Arcelin-Phytohaemagglutinin-α Amylase Inhibitor Seed Protein Locus from Tepary bean (Phaseolus acutifolius A. Gray) to Common Bean (P. vulgaris L.)." Biotechnology(Faisalabad) 8, no. 3 (June 15, 2009): 285–95. http://dx.doi.org/10.3923/biotech.2009.285.295.

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46

Fiches, Jean-Luc. "Charlette Arcelin-Pradelle, La céramique grise monochrome en Provence, 10e suppl. à la Revue archéologique de Narbonnaise, Paris, C.N.R.S., diff. De Boccard, 1984, 266 p., 73 fig., 1 plan h.t." Annales. Histoire, Sciences Sociales 40, no. 5 (October 1985): 1222–23. http://dx.doi.org/10.1017/s0395264900074953.

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47

Wanderley, Valéria S., José V. Oliveira, and Mário L. Andrade Jr. "Resistência de cultivares e linhagens de Phaseolus vulgaris L. a Zabrotes subfasciatus (Boh.) (Coleoptera: Bruchidae)." Anais da Sociedade Entomológica do Brasil 26, no. 2 (August 1997): 315–20. http://dx.doi.org/10.1590/s0301-80591997000200013.

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Avaliou-se a resistência de seis cultivares e quatro linhagens quase isogênicas de Phaseolus vulgaris a Zabrotes subfasciatus (Boh.), através de testes com e sem chance de escolha. As linhagens com arcelina apresentaram resistência do tipo antibiose, sendo a com arcelina-1 a mais resistente, pois aumentou o período de ovo a adulto em 11,9 dias e reduziu a percentagem de emergência de adultos em 86,9%, em relação a média das cultivares sem arcelina. Nenhuma das cultivares mostrou este mecanismo de resistência, porém a menor preferência para a postura no teste com chance de escolha foi observada nas cultivares Safira, IPA-7, São José e HF-465-63-1.

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BARBOSA, FLÁVIA RABELO, MASSARU YOKOYAMA, PEDRO ANTÔNIO ARRAES PEREIRA, and FRANCISCO JOSÉ PFEILSTICKER ZIMMERMANN. "Estabilidade da resistência a Zabrotes subfasciatus conferida pela proteína arcelina, em feijoeiro." Pesquisa Agropecuária Brasileira 35, no. 5 (May 2000): 895–900. http://dx.doi.org/10.1590/s0100-204x2000000500005.

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A arcelina é uma proteína encontrada em feijões silvestres e confere resistência ao caruncho-do-feijão, Zabrotes subfasciatus (Boh., 1833) (Coleoptera: Bruchidae). Comparativamente às cultivares suscetíveis Porrillo 70 e Goiano Precoce, estudou-se a estabilidade da resistência, conferida por dois alelos da proteína arcelina, nas linhagens do feijoeiro Arc1 e Arc4, após a criação do inseto por quatro gerações sucessivas no mesmo genótipo. O experimento foi conduzido no Laboratório da Embrapa-Centro Nacional de Pesquisa de Arroz e Feijão (CNPAF), no município de Santo Antônio de Goiás, GO, em condições não-controladas, utilizando-se delineamento experimental inteiramente ao acaso. Observaram-se, nas linhagens portadoras de arcelina, redução do número de ovos e de adultos emergidos, redução do peso dos insetos, e prolongamento do período ovo-adulto. Na linhagem Arc1, a resistência ao Z. subfasciatus foi mais expressiva. Nessa linhagem, os parâmetros número de ovos, número de adultos emergidos, período ovo-adulto, razão sexual e peso de machos não foram alterados, porém observou-se aumento progressivo de peso das fêmeas nas gerações. Na linhagem Arc4, houve redução do período ovo-adulto, embora o número de ovos e de adultos emergidos, razão sexual e peso de machos e fêmeas não tenham sido alterados.

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Granboulan, J. "Innovation in Arcelor." Revue de Métallurgie 102, no. 1 (January 2005): 93–102. http://dx.doi.org/10.1051/metal:2005159.

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&NA;. "Robert Arceci." Journal of Pediatric Hematology/Oncology 20, no. 2 (March 1998): 97. http://dx.doi.org/10.1097/00043426-199803000-00001.

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