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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleRegulation of lysine metabolism and endosperm protein synthesis by the opaque-5 and opaque-7 maize mutationspt_BR
dc.contributor.authorAzevedo, RApt_BR
dc.contributor.authorLea, PJpt_BR
dc.contributor.authorDamerval, Cpt_BR
dc.contributor.authorLandry, Jpt_BR
dc.contributor.authorBellato, CMpt_BR
dc.contributor.authorMeinhardt, LWpt_BR
dc.contributor.authorLe Guilloux, Mpt_BR
dc.contributor.authorDelhaye, Spt_BR
dc.contributor.authorVarisi, VApt_BR
dc.contributor.authorGaziola, SApt_BR
dc.contributor.authorGratao, PLpt_BR
dc.contributor.authorToro, AApt_BR
unicamp.authorUniv Sao Paulo, Escola Super Agr Luiz de Queiroz, Dept Genet, BR-13418900 Piracicaba, SP, Brazil Univ Sao Paulo, Ctr Energia Nucl Agr, BR-13418900 Piracicaba, SP, Brazil Univ Lancaster, Dept Biol Sci, Lancaster LA1 4YQ, England CNRS, INRA, Stn Genet Vegetale, UPS,INA,PG,UMR 8120, F-91190 Gif Sur Yvette, France INRA, Chim Biol Lab, INA PG, F-78850 Thiverval Grignon, France Univ Estadual Campinas, Dept Genet & Evolucao, BR-13081970 Campinas, SP, Brazilpt_BR
dc.subjectaspartate kinasept_BR
dc.subjectlysine 2-oxoglutarate reductasept_BR
dc.subjectstorage proteinspt_BR
dc.subject.wosReductase-saccharopine Dehydrogenasept_BR
dc.subject.wosSensitive Aspartate Kinasept_BR
dc.subject.wosBifunctional Enzymept_BR
dc.subject.wosKetoglutarate Reductasept_BR
dc.subject.wosRice Seedspt_BR
dc.subject.wosDihydrodipicolinate Synthasept_BR
dc.subject.wosTranscriptional Activatorpt_BR
dc.subject.wosHomoserine Dehydrogenasept_BR
dc.description.abstractTwo high lysine maize endosperm mutations, opaque-5 (o5) and opaque-7 (o7), were biochemically characterized for endosperm protein synthesis and lysine metabolism in immature seeds. Albumins, globulins, and glutelins, which have a high content of lysine, were shown to be increased in the mutants, whereas zeins, which contain trace concentrations of lysine, were reduced in relation to the wild-type lines B77xB79+ and B37+. These alterations in the storage protein fraction distribution possibly explain the increased concentration of lysine in the two mutants. Using two-dimensional polyacrylamide gel electrophoresis of proteins of mature grains, variable amounts of zein polypeptides were detected and considerable differences were noted between the four lines studied. The analysis of the enzymes involved in lysine metabolism indicated that both mutants have reduced lysine catabolism when compared to their respective wild types, thus allowing more lysine to be available for storage protein
dc.relation.ispartofJournal Of Agricultural And Food Chemistrypt_BR
dc.relation.ispartofabbreviationJ. Agric. Food Chem.pt_BR
dc.publisherAmer Chemical Socpt_BR
dc.identifier.citationJournal Of Agricultural And Food Chemistry. Amer Chemical Soc, v. 52, n. 15, n. 4865, n. 4871, 2004.pt_BR
dc.sourceWeb of Sciencept_BR
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