犬精浆中精氨酸酯酶对肌动蛋白及其他结构蛋白的蛋白水解活性。与胰蛋白酶和激肽释放酶的比较。

Proteolytic activity of arginine esterase from dog seminal plasma towards actin and other structural proteins. Comparison with trypsin and kallikrein.

作者信息

Frenette G, Dubé J Y, Tremblay R R

出版信息

Int J Biochem. 1986;18(8):697-703. doi: 10.1016/0020-711x(86)90392-7.

Abstract

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.

摘要

在酶/底物等摩尔比的情况下，肌动蛋白、原肌球蛋白、纤连蛋白和肌球蛋白在37℃孵育一小时期间被大量水解。犬血清白蛋白、卵清蛋白、牛γ球蛋白和人前列腺酸性磷酸酶未被水解。精氨酸酯酶在pH 6.5、7.1和7.6时对肌动蛋白的活性分别为在最佳pH 8.2时所测活性的60%、74%和84%。尽管胰蛋白酶活性高5000倍，但精氨酸酯酶和胰蛋白酶对肌动蛋白的裂解产物相似。激肽释放酶产生了精氨酸酯酶和胰蛋白酶未观察到的肌动蛋白主要片段。得出的结论是，精氨酸酯酶对结构蛋白具有低胰蛋白酶样活性，并且这种活性可能具有生理意义。