Gupta R C, Bhalla R C, Sharma R V
Biochem Pharmacol. 1982 May 15;31(10):1837-41. doi: 10.1016/0006-2952(82)90485-3.
cAMP-dependent protein kinase activity was reduced in the cytosol fraction of spontaneously hypertensive rat (SHR) aorta compared to that of the Kyoto Wistar control rat (WKY). Two major peaks, isozymes I and II, of soluble cyclic AMP-dependent protein kinase activity could be separated by DEAE-cellulose chromatography. The distributions of isozymes I and II were 40 and 60%, respectively, in WKY compared to 26 and 74% in SHR. Isozyme I of SHR eluted at a conductance of 2-3 mmhos compared to 5-6 mmhos in WKY. In addition, activity under the peak of isozyme I of SHR was reduced by approximately 55% compared to WKY. The half-life of thermal denaturation of isozyme I at 50 degrees was 21 min in WKY compared to 84 min in SHR. On the other hand, for isozyme II no significant differences were observed between WKY and SHR in elution pattern, total activity under the peak, or thermal denaturation of enzyme activity. These data suggest that specific changes had occurred in isozyme I of SHR.
与京都Wistar对照大鼠（WKY）相比，自发性高血压大鼠（SHR）主动脉胞质部分的环磷酸腺苷依赖性蛋白激酶活性降低。可溶性环磷酸腺苷依赖性蛋白激酶活性的两个主要峰，同工酶I和II，可以通过DEAE-纤维素色谱法分离。在WKY中，同工酶I和II的分布分别为40%和60%，而在SHR中分别为26%和74%。SHR的同工酶I在2-3毫姆欧的电导率下洗脱，而WKY在5-6毫姆欧下洗脱。此外，与WKY相比，SHR同工酶I峰下的活性降低了约55%。在50摄氏度下，WKY中同工酶I热变性的半衰期为21分钟，而SHR中为84分钟。另一方面，对于同工酶II，在洗脱模式、峰下总活性或酶活性的热变性方面，WKY和SHR之间未观察到显著差异。这些数据表明SHR的同工酶I发生了特定变化。
