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 …

A rapid and highly efficient procedure for purification of kininase II from human seminal
plasma is described. After ultra centrifugation, the enzyme was purified by gel filtration on …

The activity of kininase II in crude human sperm was measured continuously by measuring
the hydrolysis of a blocked tripeptide 3-(2-furylacryloyl)-L-phenylalanyl-glycl-glycine (1 …

In an experimental study the localisation and activity of hog-pancreatic Kallikrein was
investigated immunologically and enzymatically in the testis and epididymis. A concentration …

Partially purified human plasma kininase II was incubated with proteolytic enzymes such as
plasma kallikrein, prekallikrein activator, plasmin, thrombin and trypsin. Digestion of plasma …

Human plasma low molecular weight kininogen was purified with ammonium sulfate
fractionation, DEAE-cellulose, CM-Sephadex C-50 and aprotinin-agarose affinity column …

A tissue kallikrein from human seminal plasma was isolated by immunoaffinity
chromatography and characterized. Its molecular mass was determined by gel filtration to be …

A highly purified kallikrein was isolated from human urine with 43% yield and a purification
factor of 25. The enzyme is a glycoprotein with a molecular weight of 43,600. The protein is …

A method was developed to measure kininase activity in human urine. The method consists
of dialysis of human centrifuged urine sample against phosphate buffer and partial …

Abstract Kininase I (EC 3.4. 17.3) activity has been determined in human fluids and tissues
of the urogenital tract. Benzoyl-glycyl-L-arginine and benzoyl-glycyl-L-lysine were used as …