Interaction of cystatin C variants with papain and human cathepsins B, H and L

被引：40

作者：

Cimerman, N

Prebanda, MT

Turk, B

Popovic, T

Dolenc, I

Turk, V

机构：

[1] KRKA DD, Dept Biochem Res & Drug Design, Div Res & Dev, Ljubljana 1000, Slovenia

[2] Jozef Stefan Inst, Dept Biochem & Mol Biol, Ljubljana 1000, Slovenia

来源：

JOURNAL OF ENZYME INHIBITION | 1999年 / 14卷 / 02期

关键词：

cathepsins B; H; L; human cystatin C; inhibition; papain; W106S and L9-cystatin C mutants;

D O I：

10.3109/14756369909036552

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：

Recombinant human cystatin C and two of its mutants were expressed in Escherichia coli. The recombinant inhibitor was found to be identical to authentic cystatin C as judged by isoelectric focusing (pI 9.2) and kinetics of inhibition of papain and human cathepsins B, H and L. N-terminal truncation of 8 residues resulted in a decrease of isoelectric point (pI 7.8), but the inhibitory properties were similar to those of recombinant cystatin C, suggesting that Leu9 is a critical residue for the inhibition. The mutation of Trp106 to Ser, however, resulted in a decreased affinity of the inhibitor for the enzymes tested, with the largest effect on cathepsin B inhibition (similar to 100-fold increase in K(i)).

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页码：167 / 174

页数：8

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