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. 1982 Oct;70(4):1199–1209. doi: 10.1104/pp.70.4.1199

Biochemical Characterization of Canavalin, the Major Storage Protein of Jack Bean 1

Stephanie Campbell Smith 1, Stephen Johnson 1, James Andrews 1, Alexander McPherson 1
PMCID: PMC1065850  PMID: 16662638

Abstract

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 C3 and pseudo D3). 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 α-d-mannosidase activity and seems to share a number of other physical and chemical properties with that enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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