0000000000814364
AUTHOR
J.logan Irvin
Two proteases from nuclei of rat testis cells. II. Inhibitors
Abstract Proteases Rc and Kc of the nuclei of rat testis cells exhibit considerable differences in susceptibility to various protease inhibitors. Protease Rc is inhibited by D‐phenylalanyl‐L‐propyl‐L‐arginine chlormethylketone and p‐nitrophenyl‐p1‐guanidino ben‐zoate. Protease Kc is inhibited by Nα‐p‐tosyl‐L‐lysine chlormethylketone, N‐p‐tosyl‐phenylalanine chlormethylketone, N‐carbobenzoxy‐L‐phenylalanine chloromethylketone and p‐nitrophenyl‐p'‐guanidino‐benzoate. Neither protease is inhibited by 10 mM phenylmethanesulphonyl‐fluoride or p‐chloromercuri‐benzoate. p‐nitrophenyl‐p1‐guanidino‐benzoate is a substrate for protease Rc with release of p‐nitrophenol, however the protease activity i…
Two proteases from nuclei of rat testis cells. I. Isolation
Abstract Two proteases, assayed with fluorogenic peptides and tentatively designated Rc and Kc, have been isolated from nuclei of rat testis cells by differential extraction with acetic acid, removal of some proteins at pH 4.5, and polyacrylamide gel electrophoresis followed by electroblotting onto nitrocellulose paper. Protease R hydrolyzes t‐Butyl‐oxycarbonyl‐Val‐Pro‐Arg‐7‐amino‐4‐methyl‐coumarin and other peptides in which arginine is joined to 7‐amino‐4‐methyl‐coumarin by amide linkage. Protease Kc has a preference for peptides terminating in lysine‐7‐amino‐4‐methylcoumarin amide. Neither of these proteases is active against Glu‐Phe‐7‐amino‐4‐methyl‐coumarin amide or Carbobenzoxy‐Arg‐7‐…