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SUMMARY We have previously reported the presence of a cardiac kinin-generating enzyme (CKGE) in human cardiac tissue. The present study was undertaken to examine the subcellular localization and the biochemical properties of this system in rat cardiac tissue. Cardiac bomogenate (20 mg) was incubated with beattreated plasma substrate and citrate-pbospbate buffer (pH 5.3) in the presence of peptidase inhibitors, and the vasoactive substance released was tested on the isolated cat jejunum and the arterial pressure of the rat. Rat cardiac tissue contains an enzyme which releases a kinln from a substrate present in rat plasma. The klnlnreleaslng substance is nondialyzable and neat labile. The rate at which it releases kinin is similar to the rate of kinin released by kallikrein and trypsin, but it is unaffected by incubation of the enzyme with soybean trypslninhibitor or trasylol. The study of its subcellular distribution by differential centrifugation showed a similar pattern to that of acid pbosphatase. With sucrose density gradient centrifugation, the equilibrium density for the CKGE-containing particles was 1.164±0.002 g/ml and the distribution of the CKGE was also similar to that of acid phosphatase. The CKGE showed a pi of 4.5±0.2 and an apparent molecular weight of about 30,000 to 35,000 by gel filtration (Aca-54). The kinin released by cardiac homogenate resembles bradykinin in its chemical and pharmacological properties, and, by using antibodies that specifically inhibit kinins, the biological action was completely abolished. These results indicate that the subcellular distribution of the CKGE is similar to that of a lysosomal protease, and that its physicochemical characteristics differ from those of plasmatic kallikrein but are quite similar to those of kallikreins of glandular origin. (Hypertension 3 (suppl II): II-42-II-45, 1981)

Kinin-forming enzyme of rat cardiac tissue. Subcellular distribution and biochemical properties.