dc.creatorAzevedo, RA
dc.creatorDamerval, C
dc.creatorLea, PJ
dc.creatorLandry, J
dc.creatorBellato, CM
dc.creatorMeinhardt, LW
dc.creatorLe Guilloux, M
dc.creatorDelhaye, S
dc.creatorToro, AA
dc.creatorGaziola, SA
dc.creatorVarisi, VA
dc.creatorGratao, PL
dc.date2004
dc.date2014-11-13T13:10:15Z
dc.date2015-11-26T17:09:36Z
dc.date2014-11-13T13:10:15Z
dc.date2015-11-26T17:09:36Z
dc.date.accessioned2018-03-28T23:58:14Z
dc.date.available2018-03-28T23:58:14Z
dc.identifierFunctional Plant Biology. Csiro Publishing, v. 31, n. 4, n. 339, n. 348, 2004.
dc.identifier1445-4408
dc.identifierWOS:000221249800004
dc.identifier10.1071/FP03173
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/67907
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/67907
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/67907
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1280663
dc.descriptionThe capacity of three maize endosperm opaque mutants (o10, o11 and o13) to accumulate soluble lysine in the seed in relation to their wildtype counterpart, W22+, was investigated. The W22o13 and W22o11 mutants exhibited 278% and 186% increases in soluble lysine, respectively, while for W22o10, a 36% decrease was observed, compared with the wildtype. A quantitative and qualitative study of the N constituents of the endosperm has been conducted and data obtained for the total protein, non-protein N, soluble amino acids, albumins/globulins, zeins and glutelins present in the seed of the mutants. Following 2D-PAGE, a total of 38 different forms of zein polypeptides were detected and considerable differences were noted between the three mutant lines. The metabolism of lysine was also studied by analysis of the enzymes aspartate kinase, homoserine dehydrogenase, lysine 2-oxoglutarate reductase and saccharopine dehydrogenase, which exhibited major changes in activity, depending on the genotype, suggesting that the mutant genes may have distinct regulatory activities.
dc.description31
dc.description4
dc.description339
dc.description348
dc.languageen
dc.publisherCsiro Publishing
dc.publisherCollingwood
dc.publisherAustralia
dc.relationFunctional Plant Biology
dc.relationFunct. Plant Biol.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectaspartate kinase
dc.subjectlysine 2-oxoglutarate reductase
dc.subjectmaize
dc.subjectmutants
dc.subjectstorage proteins
dc.subjectReductase-saccharopine Dehydrogenase
dc.subjectBifunctional Enzyme
dc.subjectAspartate Kinase
dc.subjectTranscriptional Activator
dc.subjectHigher-plants
dc.subjectRice Seeds
dc.subjectDihydrodipicolinate Synthase
dc.subjectKetoglutarate Reductase
dc.subjectPhaseolus-vulgaris
dc.subjectOpaque-2
dc.titleGenetic control of lysine metabolism in maize endosperm mutants
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución