Glycinin A4A5 subunit digesting protease in soybean seeds.
Endopeptidase was partially purified from the globulin fraction of 4-hr-imbibed soybean seeds. The protease fraction obtained had proteolytic activity on the glycinin A4A5 subunit at both pH 4 and 8. A suitable peptidic substrate for the endopeptidase was isolated from the tryptic digest of the carboxymethylated A4A5 subunit. Using the tryptic peptide of glycinin A5 subunit, a simple assay system for the soybean endopeptidase activity has been established. The activity was significantly inhibited by phenylmethylsulfonyl fluoride, indicating the endopeptidase is a serine protease.
Akhtaruzzaman
M
M
Department of Agricultural Science, Faculty of Agriculture, Okayama University.
Kimura
Y
Y
Takagi
S
S
D000595:Amino Acid Sequence; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D005916:Globulins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D014674:Plant Proteins, Dietary / Q000378:metabolism*; D012639:Seeds / Q000201:enzymology; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D030262:Soybean Proteins; D013025:Glycine max / Q000201:enzymology*; D013379:Substrate Specificity
D005916:Globulins; D046911:Macromolecular Substances; D014674:Plant Proteins, Dietary; D030262:Soybean Proteins; C011474:glycinin; D012697:Serine Endopeptidases