Molecular Cloning and Characterization of Cystatin, a Cysteine Protease Inhibitor, from Bufo melanostictus
スポンサーリンク
概要
- 論文の詳細を見る
Cystatins are efficient inhibitors of papain-like cysteine proteinases, and they serve various important physiological functions. In this study, a novel cystatin, Cystatin-X, was cloned from a cDNA library of the skin of Bufo melanostictus. The single nonglycosylated polypeptide chain of Cystatin-X consisted of 102 amino acid residues, including seven cysteines. Evolutionary analysis indicated that Cystatin-X can be grouped with family 1 cystatins. It contains cystatin-conserved motifs known to interact with the active site of cysteine proteinases. Recombinant Cystatin-X expressed and purified from Escherichia coli exhibited obvious inhibitory activity against cathepsin B. rCystatin-X at a concentration of 8 µM inhibited nearly 80% of cathepsin B activity within 15 s, and about 90% of cathepsin B activity within 15 min. The Cystatin-X identified in this study can play an important role in host immunity and in the medical effect of B. melanostictus.
著者
-
ZHANG A-Mei
Laboratory of Molecular Virology, Faculty of Life Sciences and Technology, Kunming University of Science and Technology
-
SONG Yuzhu
Engineering Research Center for Molecular Diagnosis, Faculty of Life Science and Technology, Kunming University of Science and Technology
-
LIU Wa
Engineering Research Center for Molecular Diagnosis, Faculty of Life Science and Technology, Kunming University of Science and Technology
-
JI Senlin
Engineering Research Center for Molecular Diagnosis, Faculty of Life Science and Technology, Kunming University of Science and Technology
-
HAN Qinqin
Engineering Research Center for Molecular Diagnosis, Faculty of Life Science and Technology, Kunming University of Science and Technology
-
FENG Yue
Laboratory of Molecular Virology, Faculty of Life Sciences and Technology, Kunming University of Science and Technology