Ossikovski E, Walter R D
Mol Biochem Parasitol. 1984 Jul;12(3):299-306. doi: 10.1016/0166-6851(84)90086-0.
The occurrence of multiple protein kinases, distinguished with respect to molecular weight and preference for acceptor proteins, was demonstrated in Ascaridia galli. The molecular weights of the cyclic AMP-dependent protein kinase and of phosvitin kinase I and II - both independent of cyclic AMP-were determined to be 160000, greater than 200000 and 40000, respectively. The cyclic AMP-dependent protein kinase preferred histones and kemptide as acceptor substrates; stimulation of enzyme activity was up to 4-fold by cyclic AMP. The activities of phosvitin kinase I and II were found to be effectively inhibited by suramin. The inhibition constants were calculated to be 2 microM and 5 microM, respectively. In addition, stibophen turned out to be a potent inhibitor of phosvitin kinase I; the inhibition constant was determined to be 10 microM.
在鸡蛔虫中证实了存在多种蛋白激酶，这些蛋白激酶在分子量和对受体蛋白的偏好方面有所不同。环磷酸腺苷（cAMP）依赖性蛋白激酶以及磷蛋白激酶I和II（两者均独立于cAMP）的分子量分别确定为160000、大于200000和40000。cAMP依赖性蛋白激酶优先选择组蛋白和肯普肽作为受体底物；环磷酸腺苷可使酶活性提高4倍。发现苏拉明可有效抑制磷蛋白激酶I和II的活性。计算出的抑制常数分别为2微摩尔和5微摩尔。此外，敌百虫被证明是磷蛋白激酶I的有效抑制剂；其抑制常数确定为10微摩尔。
