首页 | 本学科首页   官方微博 | 高级检索  
     


Inactivation of bradykinin and kallidin by cathepsin G and mast cell chymase
Authors:C F Reilly  N B Schechter  J Travis
Affiliation:1. Dept. of Biochemistry , Univ. of Georgia, Athens, Georgia 30602, USA;2. Dept. of Dermatology , Univ. of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, USA
Abstract:
Human neutrophil cathepsin G and human skin chymase can inactivate bradykinin by cleavage at the carboxy terminal phenylalanyl-arginyl peptide bond of this polypeptide. The mast cell enzyme is far more effective than cathepsin G, the rates of hydrolysis being comparable to that found for angiotensin I to angiotensin II conversion (C.F. Reilly, D. Tewksbury, N. Schechter, and J. Travis, J. Biological Chemistry 257:8619-8622). This ability to both inactivate bradykinin and accelerate the production of angiotensin II may be of significance in the development of biochemical events associated with inflammation.
Keywords:
本文献已被 ScienceDirect 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号