Inactivation of human plasma α1‐proteinase inhibitor by human PMN leucocyte collagenase

FEBS Letters

Tschesche, Harald¹  Reinke, Heinz¹  Knäuper, Vera¹ 

[1] University of Bielefeld, Faculty of Chemistry, Department of Biochemistry, P.O. Box 8640, D-4800 Bielefeld 1, FRG

关键词: Polymorphonuclear leucocyte collagenase;    α1-Proteinase inhibitor;    Proteolytic inactivation;   

DOI  :  10.1016/0014-5793(90)81412-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Highly purified human polymorphonuelear leucocyte collagenase cleaved human α-1-proteinase inhibitor (α₁-PI) at the carboxyl site of Phe³⁵² (P₇). The inhibitor was thereby rapidly inactivated and generated a primary degradation product as shown by reverse-phase HPLC and N-terminal sequencing. Prolonged incubation of the modified inhibitor with polymorphonuclear leucocyte collagenase led to the generation of a secondary degradation product with additional cleavage at the carboxyl site of Pro³⁵⁷ (P₂).

【 授权许可】

Unknown