Characterization of cystatin c from bovine parotid glands: Cysteine proteinase inhibition and antiviral properties

被引：24
作者：
Cimerman, N
Kosorok, MD
Korant, BD
Turk, B
Turk, V
机构：
[1] JOZEF STEFAN INST,DEPT BIOCHEM & MOLEC BIOL,LJUBLJANA 61000,SLOVENIA
[2] DUPONT CO INC,CENT RES & DEV,EXPTL STN,WILMINGTON,DE 19880
来源：
BIOLOGICAL CHEMISTRY HOPPE-SEYLER | 1996年 / 377卷 / 01期
关键词：
antiviral effect; bovine cathepsin B; bovine cystatin C; papain;
D O I：
10.1515/bchm3.1996.377.1.19
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Cystatin C, a low M(r) cysteine proteinase inhibitor was isolated from bovine parotid glands by a procedure which includes alkaline treatment of the homogenate, affinity chromatography, gel filtration and ion exchange chromatography. The purified inhibitor has a pI of 8.0 and M(r) of 14 500. The identity with bovine cystatin C from colostrum was confirmed by N-terminal sequence of the inhibitor and amino acid composition. Cystatin C rapidly (k(ass) = 5.5 x 10(7) M(-1) s(-1)) and tightly inhibits papain (K-i = 0.02 nM), whereas its interaction with bovine cathepsin B is substantially weaker (K-i = 4.4 nM). Bovine cystatin C also shows a weak antiviral effect on poliovirus infected human Hela cells.
引用
收藏
页码：19 / 23
页数：5
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