Abstract
1. 1. At equimolar ratio of enzyme/substrate, actin, tropomyosin, fibronectin and myosin were extensively hydrolyzed during an incubation of one hour at 37°C. 2. 2. Dog serum albumin, ovalbumin, bovine γ-globulin and human prostatic acid phosphatase were not 3. 3. The activity of arginine esterase towards actin at pHs 6.5, 7.1 and 7.6 was respectively 60, 74 and 84% of the one found at optimum pH 8.2. 4. 4. The cleavage products of actin by arginine esterase and trypsin were similar although trypsin activity was 5000-fold higher. 5. 5. Kallikrein produced a major fragment of actin not observed with arginine esterase and trypsin. 6. 6. It is concluded that arginine esterase has a low trypsin-like activity towards structural proteins and that this activity may have a physiological significance.
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