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A tissue kallikrein was purified over 1500-fold from the postmicrosomal supernatant of human submaxillary glands. The purified enzyme gave a single band, corresponding to an apparent molecular weight of 42,000 on SDS-polyacrylamide gel electrophoresis. This enzyme cross-reacted with the anti-human urinary kallikrein antiserum. The purified enzyme was characterized in comparison with the purest human urinary kallikrein preparation. Both enzymes hydrolyzed the synthetic substrate, Ac-Phe-Arg-OMe, most effectively. Aprotinin, TLCK, and PMSF suppressed the enzyme activities, while SBTI, LBTI, and alpha 1-antitrypsin had no effect at all. The purified enzyme generated kinin from the natural substrate, kininogen. It was concluded therefore that the purified enzyme is a typical tissue kallikrein.
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