Amino Acid Sequences of Proteinase Inhibitors II and II′ from Adzuki Beans

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Abstract
Reduced and carboxymethylated adzuki bean proteinase inhibitors II and II′ were digested with trypsin and with staphylococcal protease. Chymotrypsin-modified and cyanogen bromide-modified inhibitors were also reduced and carboxymethylated. The amino acid sequences of the resulting peptides were determined by the Edman degradation procedure and the carboxypeptidase technique. Inhibitor II was a single chain and consisted of 81 amino acid residues. Inhibitor II′ contained 72 amino acid residues and appeared to be derived from inhibitor II by loss of 9 amino-terminal residues. These adzuki bean inhibitors were found to be highly homologous to lima bean inhibitor IV.