Cleavage specificities of individual members of kallikrein family of proteins on synthetic peptide containing the bradykinin sequence.
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.
Uddin
M
M
Department of Anatomy and Physiology, Meharry Medical College, Nashville, Tennessee 37208, USA.
Beg
O U
OU
D000818:Animals; D001920:Bradykinin / Q000737:chemistry / Q000378:metabolism*; D007610:Kallikreins / Q000302:isolation & purification / Q000378:metabolism*; D051379:Mice; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism*; D013379:Substrate Specificity
D010455:Peptides; D007610:Kallikreins; D001920:Bradykinin