The complete amino acid sequence of a subtilisin inhibitor from adzuki beans (Vigna angularis).
The complete amino acid sequence of a major molecular form of subtilisin inhibitor from adzuki beans (Vigna angularis) was established by manual analysis using 4-N,N-dimethylaminoazobenzene-4'-isothiocyanate (DABITC). Sequencing was performed on the peptides which were derived by digesting the inhibitor with lysyl-endopeptidase and Staphylococcus aureus V8-protease. The inhibitor consisted of 92 amino acid residues and the molecular weight was calculated to be 10,800. A minor form of subtilisin inhibitor was found, which lacked the amino-terminal 19 residues of the major one. Comparison of amino acid sequences revealed that the adzuki bean subtilisin inhibitors were 29-68% homologous in sequence to the inhibitors of so-called "potato inhibitor I family."
Nozawa
H
H
Department of Biological Fundamentals, Graduate School of Science and Technology, Kobe University, Hyogo.
Yamagata
H
H
Aizono
Y
Y
Yoshikawa
M
M
Iwasaki
T
T
D000595:Amino Acid Sequence; D007887:Fabaceae; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010940:Plant Proteins; D010946:Plants, Medicinal; D011480:Protease Inhibitors; D012639:Seeds; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases / Q000378:metabolism
D010446:Peptide Fragments; D010940:Plant Proteins; D011480:Protease Inhibitors; C063260:subtilisin inhibitor, Vigna angularis; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; C036813:lysyl endopeptidase