Tao M, Salas M L, Lipmann F
Proc Natl Acad Sci U S A. 1970 Sep;67(1):408-14. doi: 10.1073/pnas.67.1.408.
Two protein phosphokinases (EC 2.7.1.37) were found to be present in rabbit reticulocytes. The two enzymes were separated by DEAE-cellulose chromatography and called kinases I and II. Adenosien 3':5'-cyclic monophosphate stimulated the activity of both enzymes. However, the degree of stimulation was different and depended on the protein acceptor used. In the presence of adenosine 3':5'-cyclic monophosphate, protein kinase I dissociated into two subunits: a subunit binding adenosine 3':5'-cyclic monophosphate, and a catalytic subunit. The component binding the cyclic nucleotide appeared to act as an inhibitory protein, regulating the activity of the catalytic subunit. The mechanism of action of the cyclic nucleotide on kinase II appeared to be different from that of kinase I.
在兔网织红细胞中发现了两种蛋白磷酸激酶(EC 2.7.1.37)。这两种酶通过二乙氨基乙基纤维素色谱法分离,分别称为激酶I和激酶II。3':5'-环磷酸腺苷可刺激这两种酶的活性。然而,刺激程度有所不同,且取决于所使用的蛋白质受体。在3':5'-环磷酸腺苷存在的情况下,蛋白激酶I解离为两个亚基:一个结合3':5'-环磷酸腺苷的亚基和一个催化亚基。结合环核苷酸的成分似乎起到抑制蛋白的作用,调节催化亚基的活性。环核苷酸对激酶II的作用机制似乎与激酶I不同。