Histochemical localization of kallikrein-like Pro-Phe-Arg-naphthylester esterase activity in the rat kidney.
In the rat kidney the presence of the kallikrein-like pro-phe-argnaphthylester esterase activity was demonstrated by a simultaneous coupling azo dye method. The enzyme was identified as a serine-protease because it was inhibited by preincubation with diisopropyl-fluorophosphate and unaffected by sodium iodoacetate. Since kallikrein is a serine-protease and prophe-arg-naphthylester is a synthetic and sensitive substrate for kallikrein, the enzyme activity revealed by this method was considered to represent kallikrein, although non-kallikrein esterase activity is not totally excluded. The enzyme activity was localized mainly in the outer stripe of the outer medulla, with focal extensions primarily only in the lower half of the cortex corresponding to the medullary rays.
D000818:Animals; D010450:Endopeptidases / Q000378:metabolism; D006651:Histocytochemistry; D007531:Isoflurophate / Q000494:pharmacology; D007610:Kallikreins / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D012697:Serine Endopeptidases
D007531:Isoflurophate; D010450:Endopeptidases; D007610:Kallikreins; D012697:Serine Endopeptidases