Flotow H, Wheldrake J F
School of Biological Sciences, Flinders University of South Australia, Bedford Park.
Mol Cell Biochem. 1987 Dec;78(2):141-50. doi: 10.1007/BF00229688.
The cellular slime mould Polysphondylium violaceum contains a cAMP-dependent protein kinase resembling the mammalian type I enzyme. The appearance of this enzyme is developmentally regulated. The level of kinase activity is very low in vegetative cell and increases more than tenfold during differentiation. The catalytic subunit of this cAMP-dependent protein kinase has a native molecular weight of 60-80 kDa, an isoelectric point of 5.7 and an apparent Km for ATP and Kemptide of 50 and 13.4 microM respectively. It is characterised by its sensitivity to a synthetic inhibitor specific for cAMP-dependent protein kinase. The regulatory subunit has a molecular weight of 50 kDa.
细胞黏菌紫多头绒泡菌含有一种类似于哺乳动物I型酶的环磷酸腺苷（cAMP）依赖性蛋白激酶。这种酶的出现受发育调控。激酶活性水平在营养细胞中非常低，在分化过程中增加了十多倍。这种cAMP依赖性蛋白激酶的催化亚基天然分子量为60 - 80 kDa，等电点为5.7，对ATP和肯普肽的表观Km分别为50和13.4微摩尔。它的特点是对一种对cAMP依赖性蛋白激酶特异的合成抑制剂敏感。调节亚基的分子量为50 kDa。
