Interaction of human cathepsin C with chicken cystatin

被引：23

作者：

Dolenc, I ^{[1
]}

Turk, B ^{[1
]}

Kos, J ^{[1
]}

Turk, V ^{[1
]}

机构：

[1] BIOMED CTR,DEPT VET MED CHEM,S-75123 UPPSALA,SWEDEN

来源：

FEBS LETTERS | 1996年 / 392卷 / 03期

关键词：

cathepsin C; dipeptidyl aminopeptidase I; cysteine proteinase; chicken cystatin; binding stoichiometry;

D O I：

10.1016/0014-5793(96)00828-9

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：

Cathepsin C was purified from human spleen by a rapid procedure, which included homogenization, ammonium sulfate precipitation, gel filtration on Sephacryl S-200 and finally affinity chromatography on chicken cystatin-Sepharose. The interaction between cathepsin C and chicken cystatin was further characterized, It was found to be accompanied by a maximum decrease in fluorescence emission intensity at 330 nm, Fluorescence titration showed that human cathepsin C can bind four chicken cystatin molecules, The 4:1 binding stoichiometry was confirmed by titration monitored by the loss of enzyme activity, A non-competitive-competitive type of inhibition was determined from a double-reciprocal Lineweaver-Burk plot with a K-i value of 0.22 nM for the non-competitive inhibition.

引用

页码：277 / 280

页数：4

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