胱抑素对组织蛋白酶S的紧密结合抑制作用。
Tight-binding inhibition of cathepsin S by cystatins.
作者信息
Brömme D, Rinne R, Kirschke H
机构信息
Institute of Biochemistry, Faculty of Medicine, Martin-Luther University, Halle (Saale), Germany.
出版信息
Biomed Biochim Acta. 1991;50(4-6):631-5.
PMID:1801734
Abstract
Human cystatins A, B and C were purified, and their inhibition efficiency was tested with the cysteine proteinase cathepsin S. Cathepsin S was strongly inhibited by cystatins A and B in the subnanomolar range and by cystatin C in the picomolar range. Two steps of inhibition of cathepsin S by the cystatins which involve slow binding are discussed.
摘要
纯化了人胱抑素A、B和C，并测试了它们对半胱氨酸蛋白酶组织蛋白酶S的抑制效率。组织蛋白酶S在亚纳摩尔范围内被胱抑素A和B强烈抑制，在皮摩尔范围内被胱抑素C强烈抑制。讨论了胱抑素对组织蛋白酶S的两步抑制作用，这涉及到缓慢结合。
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