AMINO-ACID SEQUENCES OF PROTEINASE INHIBITOR-II AND PROTEINASE-II' FROM ADZUKI BEANS

Reduced and carboxymethylated adzuki bean proteinase inhibitors II and II' were digested with trypsin and with staphylococcal protease. Chymotrypsin-modified and cyanogen bromidemodified inhibitors were also reduced and carboxymethylated. The amino acid sequences of the resulting peptides were determined by the Edman degradation procedure and the carboxypeptidasetechnique. 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. © 1979 Taylor & Francis Group, LLC.