Purvis K, Hansson V
Int J Androl. 1980 Dec;3(6):713-8. doi: 10.1111/j.1365-2605.1980.tb00158.x.
Three different, calmodulin-dependent, isoenzymes of cyclic nucleotide phosphodiesterase (PDE) can be isolated by DEAE cellulose chromatography from the immature rat testis and shown to have different substrate specificities and kinetic behaviour. Calmodulin is regulating the activity of these enzymes by altering the maximal velocity (Vmax) rather than the Km of the reaction. Two of the 3 enzymes appear to be testis-specific, while the remaining possesses properties similar to that described for the calmodulin-dependent PDE found in other tissue.
通过DEAE纤维素色谱法可从未成熟大鼠睾丸中分离出三种不同的、钙调蛋白依赖性的环核苷酸磷酸二酯酶(PDE)同工酶,它们具有不同的底物特异性和动力学行为。钙调蛋白通过改变反应的最大速度(Vmax)而非米氏常数(Km)来调节这些酶的活性。这三种酶中的两种似乎是睾丸特异性的,而另一种具有与其他组织中发现的钙调蛋白依赖性PDE相似的特性。