Proteolytic activity of arginine esterase from dog seminal plasma towards actin and other structural proteins. Comparison with trypsin and kallikrein.
At equimolar ratio of enzyme/substrate, actin, tropomyosin, fibronectin and myosin were extensively hydrolyzed during an incubation of one hour at 37 degrees C. Dog serum albumin, ovalbumin, bovine gamma-globulin and human prostatic acid phosphatase were not hydrolyzed. 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. The cleavage products of actin by arginine esterase and trypsin were similar although trypsin activity was 5000-fold higher. Kallikrein produced a major fragment of actin not observed with arginine esterase and trypsin. It is concluded that arginine esterase has a low trypsin-like activity towards structural proteins and that this activity may have a physiological significance.
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001798:Blood Proteins / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D004285:Dogs; D007610:Kallikreins / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D009124:Muscle Proteins / Q000378:metabolism*; D012661:Semen / Q000201:enzymology*; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism*
D000199:Actins; D001798:Blood Proteins; D009124:Muscle Proteins; C019724:arginine esterase; D002265:Carboxylic Ester Hydrolases; D007610:Kallikreins; D014357:Trypsin