title: Cleavage specificities of individual members of kallikrein family of proteins on synthetic peptide containing the bradykinin sequence.
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.
authors.affiliation: Department of Anatomy and Physiology, Meharry Medical College, Nashville, Tennessee 37208, USA.
authors.forename: M
authors.initials: M
authors.lastname: Uddin
authors.forename: O U
authors.initials: OU
authors.lastname: Beg
mesh_terms: 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
chemical_list: D010455:Peptides; D007610:Kallikreins; D001920:Bradykinin