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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-6-29
pubmed:abstractText
The structure of canavalin, a jack bean (Canavalis ensiformis) protein homologous to phaseolin, the major seed storage protein of Phaseolus vulgaris, has been investigated by x-ray crystallography and found to be a hexamer composed of three identical pairs of similar but nonidentical subunits related by a perfect 3-fold axis and pseudo dyad axes (strict C(3) and pseudo D(3)). One member of each pair of subunits is derived from the amino terminal half of a precursor polypeptide of molecular weight 49,000 and the other from its carboxy terminal half. Thus, the crystallographic evidence indicates that the precursor polypeptide is a tandem duplicate and is structurally redundant (McPherson A. 1982 J Biol Chem 255: 10472). A number of physical and chemical properties of the protein in both the uncleaved and the cleaved form were investigated. These included the native molecular weights, amino acid analyses, number of exposed sulfhydryl groups, carbohydrate content, metal ion analysis, crystallization behavior, and the fate of the protein in developing seeds. It was also found that the purified precursor protein possesses a substantial level of alpha-d-mannosidase activity and seems to share a number of other physical and chemical properties with that enzyme.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Oct
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1199-209
pubmed:dateRevised
2010-9-14
pubmed:year
1982
pubmed:articleTitle
Biochemical characterization of canavalin, the major storage protein of jack bean.
pubmed:affiliation
Department of Biochemistry, University of California, Riverside, California 92521.
pubmed:publicationType
Journal Article