Limited proteolysis of Cl‐inhibitor by chymotrypsin‐like proteinases

FEBS Letters

Schechterf, Norman M.¹  Cooperman, Barry S.⁴  Schoenberger, Oeyvind L.⁴  Rubin, Harvey³  Sprows, Jennifer L.² 

[1] From the Departments of Biochemistry and Biophysics , University of Pennsylvania, Philadelphia PA 19104, USA;From the Departments of Dermatology, University of Pennsylvania, Philadelphia PA 19104, USA;From the Departments of Medicine, University of Pennsylvania, Philadelphia PA 19104, USA;From the Departments of Chemistry, University of Pennsylvania, Philadelphia PA 19104, USA

关键词: Cl-inhibitor;    Limited proteolysis;    Chymotrypsin-like proteinase;    N-terminal sequence;   

DOI  :  10.1016/0014-5793(89)81519-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Limited proteolysis of Cl-inhibitor was observed with human skin chymase, human cathepsin G, and bovine chymotrypsin. In each case, the inhibitor was degraded to one major product migrating slightly faster than the native inhibitor in an SDS-polyacrylamide gel. The inhibitory activity of Cl-inhibitor against human plasma kallikrein was not altered by the modification with chymase. Edman degradation of the proteolyzed inhibitor revealed two sequences in a 1:1 ratio: NPNATSSSQ, the N-terminus of native Cl-inhibitor, and VEPILEVSSL. This second sequence showed that the Phe³³-Val³⁴ bond was hydrolyzed. Our results provide another example of the susceptibility of the N-terminal region of Cl-inhibitor to proteolytic cleavage.

【 授权许可】

Unknown