Linked Life Data

8951029

Source:http://linkedlifedata.com/resource/pubmed/id/8951029

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-1-16
pubmed:abstractText
The 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) Mol. 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 posttranslational 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
336
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Amino acid sequence of a new 2S albumin from Ricinus communis which is part of a 29-kDa precursor protein.
pubmed:affiliation
Departamento de Bioquímica, Universidade Federal do Rio de Janeiro, Brazil.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't