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Updated: Aug 17, 2026
Isolation and Identification of Bacterial Strains from Skin of Terrestrial Amphibians
Published on: June 17, 2025
Isolation and preliminary characterization of a 22-kDa protein with trypsin inhibitory activity from toad Bufo
Yu Zhao1, Yang Jin, Wen-Hui Lee
1Department of Animal Toxinology, Kunming Institute of Zoology, The Chinese Academy of Sciences, 32 East Jiao Chang Road, Kunming, Yunnan 650223, People's Republic of China.
Abstract:
A novel trypsin inhibitor termed BATI was purified to homogeneity from the skin extracts of toad Bufo andrewsi by successive ion-exchange, gel-filtration and reverse-phase chromatography. BATI is basic single chain glycoprotein, with apparent molecular weight of 22 kDa in SDS-PAGE. BATI is a thermal stable competitive inhibitor and effectively inhibits trypsin's catalytic activity on peptide substrate with the inhibitor constant (K(i)) value of 14 nM and shows no inhibitory effect on chymotrypsin, thrombin and elastase. The N-terminal sequence of BATI is EKDSITD, which shows no similarity with other known trypsin inhibitors.
