Abstract
Following the activation of hog kidney cortex homogenate with acetone, kallikrein was purified about 317-fold by diethylaminoethyl-cellulose adsorption, acetone precipitation and chromatography on Sephadex G-75, diethylaminoethyl-Sephadex A-50 and Sephadex G-100, and affinity chromatography on Trasylol-Sepharose 4B. The final purified preparation of hog renal kallikrein had a kinin-forming activity of 35.1 μg bradykinin eq/min/mg, and appeared to be homogeneous in polyacrylamide gel electrophoresis. This enzyme was a glycoprotein with a molecular weight of 50000 as determined by gel filtration on a column of Sephadex G-100. The hog renal kallikrein had an optimum pH of 9.5 and was stable at pH 8.0. This enzyme was hardly inhibited by soybean trypsin inhibitor, but was moderately sensitive to ovomucoid and more sensitive to Kunitz inhibitor. These properties were compared with those of hog pancreatic kallikrein.
