首页 | 本学科首页   官方微博 | 高级检索  
     


Cleavage Specificities of Individual Members of Kallikrein Family of Proteins on Synthetic Peptide Containing the Bradykinin Sequence
Authors:Mukarram Uddin and Obaid U. Beg
Affiliation:(1) Department of Anatomy and Physiology, Meharry Medical College, Nashville, Tennessee, 37208;(2) Molecular Biology Core Facility, Department of Microbiology, Meharry Medical College, Nashville, Tennessee, 37208
Abstract:We have analyzed the effect on bond specificity of various isolated members of the mouse kallikrein family of proteins on a synthetic peptide containing the bradykinin sequence. The cleavage pattern shows the selected specificity of these proteases toward the synthetic peptide. The Phe–His bond (positions 11–12) in the synthetic peptide was favorably cleaved by most of the members in this family, including gamma nerve growth factor. On the other hand, the Lys–Arg bond (position 3–4) was found to be susceptible only to gamma-NGF. The combination of these cleavages could result in the degradation of bradykinin in vivo.
Keywords:Mouse kallikreins  EGF-binding proteins  bradykinin    /content/xw144652l8006404/xxlarge947.gif"   alt="  gamma"   align="  MIDDLE"   BORDER="  0"  >-NGF
本文献已被 SpringerLink 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