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dc.contributor.authorSilva, J. G.
dc.contributor.authorMachado, OLT
dc.contributor.authorIzumi, C.
dc.contributor.authorPadovan, Julio Cesar [UNIFESP]
dc.contributor.authorChait, B. T.
dc.contributor.authorMirza, U. A.
dc.contributor.authorGreene, Lewis Joel [UNIFESP]
dc.date.accessioned2018-06-15T13:55:59Z
dc.date.available2018-06-15T13:55:59Z
dc.date.issued1996-12-01
dc.identifierhttp://dx.doi.org/10.1006/abbi.1996.0526
dc.identifier.citationArchives Of Biochemistry And Biophysics. San Diego: Academic Press Inc Jnl-comp Subscriptions, v. 336, n. 1, p. 10-18, 1996.
dc.identifier.issn0003-9861
dc.identifier.urihttp://repositorio.unifesp.br/11600/42640
dc.description.abstractThe isolation and sequence determination of a new 2S albumin storage protein from Ricinus communis seeds denoted 2S ASP-Ib are described, The fragment approach using selective enzymatic cleavage, Edman degradation, and mass spectrometry was used to demonstrate that the 11-kDa heterodimer protein linked by disulfide bridges has the following structure: short chain, GEREGSSSQQCRQEVQRKDLSSCERYLRQSSS; long chain, <QQQESQQLQQCCNQVKQVRDECQCEAIKYIAEDQIQQGQLHGEESERVAQRAGEIVSSCGVRCMR. The molecular weight of the intact protein, 11,140 +/- 2, determined by matrix-assisted laser desorption mass spectrometry was consistent with the assigned structure, The S- and L-chains are identical to residues 18-49 and 66-130 of the precursor protein predicted by S., D., Irwin, J, N, Keen, J,B. C, Findlay, and J,M, Lord [(1990) Mel. Gen. Genet. 222, 400-408], on the basis of the structure of a cDNA isolated using probes based on the sequence of another 2S albumin, described by F, S., Sharief and S, S, L, Li [(1982) J. Biol. Chem. 257, 14753-14759], which we denote 2S ASP-Ia, Three of the four termini could have been produced by post-translational processing by endopeptidase(s) and carboxypeptidase(s) which utilized basic residues as the cleavage sites. Mass spectrometric evidence suggested that the protein presented microheterogeneity at its termini, i,e,, truncated forms presumably due to processing heterogeneity, The present characterization of the 2S ASP-Ib protein, the second 2S albumin from Ricinus communis seeds, demonstrates that the 237-residue precursor protein codes for two different heterodimer proteins containing 97 and 99 residues each, This system should be useful for studying the posttranslational processing of plant storage proteins. (C) 1996 Academic Press, Inc.en
dc.format.extent10-18
dc.language.isoeng
dc.publisherAcademic Press Inc Jnl-comp Subscriptions
dc.relation.ispartofArchives Of Biochemistry And Biophysics
dc.rightsAcesso restrito
dc.subject2S albuminen
dc.subjectRicinus communisen
dc.subjectstorage proteinen
dc.subjectposttranslational processingen
dc.subjectprecursor proteinen
dc.subject2S ASP-Iaen
dc.subject2S ASP-Iben
dc.titleAmino acid sequence of a new 2S albumin from Ricinus communis which is part of a 29-kDa precursor proteinen
dc.typeArtigo
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal do Rio de Janeiro (UFRJ)
dc.contributor.institutionUNIV FED RURAL RIO DE JANEIRO
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionROCKEFELLER UNIV
dc.description.affiliationUNIV SAO PAULO,FAC MED RIBEIRAO PRETO,CTR QUIM PROT,BR-14049900 RIBEIRAO PRET,SP,BRAZIL
dc.description.affiliationFED UNIV RIO DE JANEIRO,INST QUIM,DEPT BIOQUIM,BR-21949900 RIO JANEIRO,BRAZIL
dc.description.affiliationUNIV FED RURAL RIO DE JANEIRO,INST CIENCIAS EXATAS,DEPT QUIM,RIO JANEIRO,BRAZIL
dc.description.affiliationFED UNIV RIO DE JANEIRO,CTR CIENCIAS SAUDE,INST CIENCIAS BIOMED,DEPT BIOQUIM MED,BR-21910000 RIO JANEIRO,BRAZIL
dc.description.affiliationESCOLA PAULISTA MED,DEPT BIOFIS,BR-04023900 SAO PAULO,SP,BRAZIL
dc.description.affiliationROCKEFELLER UNIV,MASS SPECTROMETRY LAB,NEW YORK,NY 10021
dc.description.affiliationUNIV SAO PAULO,FAC MED RIBEIRAO PRETO,DEPT GINECOL & OBSTET,BR-14049900 RIBEIRAO PRET,SP,BRAZIL
dc.description.affiliationUnifespESCOLA PAULISTA MED,DEPT BIOFIS,BR-04023900 SAO PAULO,SP,BRAZIL
dc.identifier.doi10.1006/abbi.1996.0526
dc.description.sourceWeb of Science
dc.identifier.wosWOS:A1996VW84800002


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