Cloning and prokaryotic expression of Chinese sturgeons cystatin cDNA

文献类型： 外文期刊

第一作者： Bai, J.

作者： Bai, J.;Ma, D.;Lao, H.;Jian, Q.;Ye, X.;Luo, J.

作者机构：

关键词： Acipenser sinensis;cystatin;prokaryotic expression;protease inhibitory activity

期刊名称：Proceedings of the 13th International Congress on Genes, Gene Families and Isozymes

ISSN：

年卷期： 2005 年

页码：

收录情况： SCI

摘要： Cystatin, which is widely distributed in both animal and plant tissues and body fluids, can form activity-inhibitor complexes with cysteine proteases. In order to explore the functions of fish cystatin and its potential values in fish disease prevention and cure, as well as seafood process industry, we cloned the mature peptide cDNA of Chinese sturgeon (Acipenser sinensis) cystatin by RT-PCR method. Nucleotide sequence analysis showed that the cloned cDNA encodes 112 amino acid residues of the mature cystatin peptide and which is the homolog of the mammalian cystatin Family II, cystatin C. Using prokaryotic expression vector pBV220, a cystatin E.coli expression bacteria was constructed. After temperature inducement and SDS-PAGE analysis, the recombinant expression bacteria produced a special protein about 12 kD in molecular weight. The proportion of the recombinant protein in total bacterial protein was about 25%. The inhibitory activity of the recombinant cystatin was measured by inhibiting the protease activity of papain, and the result showed the specific inhibitory activities for the recombinant cystatin was calculated to be 48U/mg, where U is defined as mu g papain inhibied pre mu g inhibitor.

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