Fakunding J L, Means A R
Endocrinology. 1977 Nov;101(5):1358-68. doi: 10.1210/endo-101-5-1358.
The Sertoli cell of the rat testis contains two cytoplasmic forms of adenosine 3',5' monophosphate (cyclic AMP)-dependent protein kinase, designated as Peak I and Peak II, which change in relative proportion during Sertoli cell maturation. Peak I and Peak II differ in their subunit interaction. Thus, while the substrates, ATP and histone, affect cyclic AMP binding to Peak I, neither of these compounds affect the binding of cyclic AMP to the Peak II enzyme. The effects of cyclic AMP binding to Peak I appear to be due to the fact that histone and high ionic strength cause dissociation of the Peak I holoenzyme, whereas ATP stabilizes the holoenzyme complex against dissociation. The Peak II holoenzyme is not affected by either salt of histone and is only dissociated by cyclic AMP. Once dissociated, the subunits of Peak II will rapidly reassociate under low salt conditions whereas the subunits of Peak I will not reassociate. By utilizing the distinct properties of Peak I and Peak II, it is possible to demonstrate the activation of both Peak I and Peak II Sertoli cell protein kinase in response to FSH.
大鼠睾丸的支持细胞含有两种细胞质形式的3',5'-环磷酸腺苷（环磷腺苷）依赖性蛋白激酶，分别称为峰I和峰II，它们在支持细胞成熟过程中相对比例会发生变化。峰I和峰II在亚基相互作用方面存在差异。因此，虽然底物、ATP和组蛋白会影响环磷腺苷与峰I的结合，但这些化合物均不影响环磷腺苷与峰II酶的结合。环磷腺苷与峰I结合的影响似乎是由于组蛋白和高离子强度导致峰I全酶解离，而ATP可稳定全酶复合物以防解离。峰II全酶不受盐或组蛋白的影响，仅被环磷腺苷解离。一旦解离，峰II的亚基在低盐条件下会迅速重新结合，而峰I的亚基则不会重新结合。利用峰I和峰II的不同特性，可以证明支持细胞蛋白激酶峰I和峰II在促卵泡激素（FSH）作用下均被激活。
