Purification, characterization, and crystallization of single molecular species of beta-conglycinin from soybean seeds
1996
Morita, S. (fujioil-co) | Fukase, M. | Yamaguchi, M. | Fukuda, Y. | Morita, Y.
Four major molecular species of beta-conglycinin, alpha3, alpha2beta, alphabeta2, and beta3, were isolated and purified from seeds of an alpha' subunit-deficient strain of soybeans (Glycine max). All components were found to be homogeneous by high pressure liquid chromatography, SDS-polyacrylamide gel electrophoresis, and amino acid and amino terminal sequence analyses. The amino acid compositions of the alpha3 and beta3 components agreed fairly well with the compositions deduced from the cDNA sequences, and all of the components were highly glycosylated. The alpha3 and beta3 components were compared regarding their secondary structures. The secondary structure of the alpha3 component deduced from CD measurements showed a higher alpha-helix content than that of the beta3 component. The beta3 component was crystallized by decreasing the ionic strength from 0.5 to 0.14 in phosphate buffer, pH 7.3, and the crystals grew to a size (1.0 mm x 0.2 mm x 0.2 mm) suitable for X-ray crystallographic analysis. A preliminary X-ray analysis showed that the crystal belonged to an orthorhombic crystal system having the space group P212121 and unit cell dimensions of a = 185.1 A, b = 107.9 A and c = 97.6 A
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