Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10880194 | Toxicon | 2005 | 6 Pages |
Abstract
Amphibian skin secretions contain many bioactive compounds. In the present work, an irreversible serine protease inhibitor, termed baserpin, was purified for the first time from the skin secretions of toad Bufo andrewsi by successive ion-exchange and gel-filtration chromatography. Baserpin is a single chain glycoprotein, with an apparent molecular weight of about 60Â kDa in SDS-PAGE. Baserpin is an irreversible inhibitor and effectively inhibits the catalytic activity of trypsin, chymotrypsin and elastase. SDS-stable baserpin-trypsin complex could be seen in SDS-PAGE indicates that it possibly belongs to the serpin superfamily. According to the association rates determined, baserpin is a potent inhibitor of bovine trypsin (4.6Ã106Â Mâ1Â sâ1), bovine chymotrypsin (8.9Ã106Â Mâ1Â sâ1) and porcine elastase (6.8Ã106Â Mâ1Â sâ1), whereas it shows no inhibitory effect on thrombin. The N-terminal sequence of baserpin is HTQYPDILIAKPXDK, which shows no similarity with other known serine protease inhibitors.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry, Genetics and Molecular Biology (General)
Authors
Yu Zhao, Yang Jin, Shuang-Shuang Wei, Wen-Hui Lee, Yun Zhang,