Identification of the Reactive Site of Potato Proteinase Inhibitor II-b for Bovine Chymotrypsin and a Bacterial Proteinase
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A single peptide bond of potato proteinase inhibitor II-b is selectively split by a catalytic quantity of TLCK-treated bovine chymotrypsin [EC 3. 4. 4. 5] at pH 3. Fragmentation of the chymotrypsin-modified inhibitor by reduction and S-carboxymeth-ylation, followed by gel nitration through Sephadex G-50, reveals that the specific peptide bond cleaved is the Lys-Ser bond of residues 63 and 64 in the inhibitor molecule. The modified inhibitor retains the full activity of native inhibitor Il-b. However, it shows decreased activities against bovine chymotrypsin and a bacterial proteinase, Nagarse, on elimination of the newly formed carboxyl-terminal lysine from the molecule. The losses of activities against the two enzymes almost parallel the extent of removal of lysine. Therefore, it is concluded that the Lys-Ser bond of residues 63 and 64 in inhibitor II-b is the main reactive site of the inhibitor for both chymotrypsin and Nagarse.
- 社団法人 日本生化学会の論文
社団法人 日本生化学会 | 論文
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