Krizanová O
Acta Virol. 1979 Jul;23(4):303-13.
As revealed by spectrophotometry, native but not heat-inactivated influenza virus in the presence of ATP reduced the activity of calcium-dependent regulator protein-stimulated 3',5'-c AMP-phosphodiesterase (CDR-PDE). ATP could be partially replaced by ADP but not by AMP. The degree of CDR-PDE inhibition increased with increasing virus concentration. But at very high virus concentrations the rate of 3',5'-c AMP hydrolysis by CDR-PDE was not linearly dependent on time. At appropriate virus concentrations the degree of inhibition of CDR-PDE activity remained unchanged for the whole reaction time.
通过分光光度法显示，在ATP存在下，天然的而非热灭活的流感病毒降低了钙依赖性调节蛋白刺激的3',5'-环磷酸腺苷磷酸二酯酶（CDR-PDE）的活性。ATP可部分被ADP替代，但不能被AMP替代。CDR-PDE的抑制程度随病毒浓度增加而增加。但在非常高的病毒浓度下，CDR-PDE水解3',5'-环磷酸腺苷的速率与时间并非呈线性相关。在适当的病毒浓度下，整个反应时间内CDR-PDE活性的抑制程度保持不变。
