Ghazarian J G, Yanda D M
Biochem Biophys Res Commun. 1985 Nov 15;132(3):1095-102. doi: 10.1016/0006-291x(85)91919-9.
Partially purified chick kidney mitochondrial Type II protein kinase catalyzes the phosphorylation of 1 alpha-hydroxylase cytochrome P-450 without affecting the rate of product formation in vitro when 1 alpha-hydroxylase activity is reconstituted by the addition of [ferredoxin] and [ferredoxin reductase] to the phosphorylated cytochrome. The cytochrome's effective concentration, or its general spectral properties did not change upon phosphorylation. However, when the cytochrome and its ferredoxin were present simultaneously during the phosphorylation reaction, reconstitution of 1 alpha-hydroxylase activity by the addition of ferredoxin reductase failed to catalyze product formation. Although a several fold increase in the kinase activity could be demonstrated in the presence of cAMP, the above phosphorylation effects appear to be cAMP-independent.
部分纯化的鸡肾线粒体II型蛋白激酶催化1α-羟化酶细胞色素P-450的磷酸化，当通过向磷酸化的细胞色素中添加[铁氧化还原蛋白]和[铁氧化还原蛋白还原酶]来重建1α-羟化酶活性时，在体外不影响产物形成的速率。细胞色素的有效浓度或其一般光谱特性在磷酸化后没有改变。然而，当在磷酸化反应期间细胞色素及其铁氧化还原蛋白同时存在时，通过添加铁氧化还原蛋白还原酶来重建1α-羟化酶活性不能催化产物形成。尽管在cAMP存在的情况下可以证明激酶活性有几倍的增加，但上述磷酸化作用似乎与cAMP无关。
