Proteins of the kallikrein-kinin system in human semen. Isolation and properties of kininase II.
A rapid and highly efficient procedure for purification of kininase II from human seminal plasma is described. After ultracentrifugation, the enzyme was purified by gel filtration on Sepharose 6B CL and ion exchange chromatography followed by affinity chromatography of EDTA-inhibited enzyme on bradykinin-Sepharose. The enzyme was specifically inhibited by Captopril and BPP9a but not by phosphoamidon. PAGE in the presence of sodium dodecyl sulfate under reducing conditions resulted in two major protein bands with apparent molecular masses of about 55 kDa and 65 kDa and two faint protein bands at higher molecular masses. Antibodies raised against the major protein bands showed full cross reactivity with all four protein bands. The presented data indicate that kininase II of subunits.
Miska
W
W
Department of Dermatology and Andrology, Justus-Liebig-University of Giessen, Germany.
Croseck
H
H
Schill
W B
WB
D000806:Angiotensin-Converting Enzyme Inhibitors; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D008297:Male; D008970:Molecular Weight; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry / Q000302:isolation & purification*; D012661:Semen / Q000201:enzymology*; D012995:Solubility; D014461:Ultracentrifugation
D000806:Angiotensin-Converting Enzyme Inhibitors; D007703:Peptidyl-Dipeptidase A