PREPARATIVE REVERSED-PHASE HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY OF SOYBEAN PROTEINS AND CHARACTERIZATION OF FRACTIONS BY GEL-ELECTROPHORESIS

被引：21
作者：
WOLF, WJ
PETERSON, RE
SCHAER, ML
机构：
[1] Biopolymer Research, National Center for Agricultural Utilization Research, Agricultural Research Service, U.S. Department of Agriculture, 1815 North University Street, Peoria
[2] Bioactive Constituents Research, National Center for Agricultural Utilization Research, Agricultural Research Service, U.S. Department of Agriculture, 1815 North University Street, Peoria
来源：
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 1992年 / 40卷 / 10期
关键词：
D O I：
10.1021/jf00022a016
中图分类号：
S [农业科学];
学科分类号：
09 ;
摘要：
Preparative (100-200 mg) reversed-phase high-performance liquid chromatography was conducted on water-extractable, acid-precipitated, and whey proteins plus purified beta-conglycinin and glycinin from soybeans. Chromatographic fractions were collected, freeze-dried, and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Polypeptide profiles obtained by electrophoresis of the fractions indicated that glycinin and beta-conglycinin, the two major storage proteins, separated only partially. Glycinin subunit G5 (A3B4) Was the first of these two proteins to elute followed by three other glycinin subunits. As elution of glycinin subunits continued, they were accompanied by beta-conglycinin. Apparently, glycinin subunits and beta-conglycinin do not differ sufficiently in hydrophobicity to permit their complete separation. Elution behaviors of minor proteins including Kunitz trypsin inhibitor and agglutinin were also determined.
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页码：1809 / 1816
页数：8
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