Kallikreinlike activity in perfusates and urine of isolated rat kidneys

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Abstract
In the perfusate and the urine produced during perfusion of isolated rat kidneys a kallikrein-like enzyme similar to that found in the kidneys was detectable by bioassay 15-25 min after the beginning of the perfusion. The source of the kallikrein activity was the kidney itself, since before the perfusion was started the blood remaining in the kidneys was washed out, and the perfusion medium was free of kallikrein and its precursors and substrates. The kallikreinlike activity of the perfusate was characterized by an oxytocic effect on isolated rat uterus, a kininogenase activity on kininogen II, an esterase activity on N-benzoyl-L-arginine ethyl ester and a hypotensive effect on anesthetized rats. These properties were inhibited by diisopropyl fluorophosphate and aprotinin but not by pepstatin. Kallikreinlike activity in the perfused kidney was lower than that in the nonperfused organ, but the total amount of kallikrein activity released to the excreted urine and the perfusate was significantly greater than the corresponding activity that disappeared in the kidney. This result agrees with the concept that the renal tissue can synthesize kallikrein.

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