期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1970
卷号：67
期号：1
页码：408-414
DOI：10.1073/pnas.67.1.408
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
