Activation of protein kinase isoenzymes under near physiological conditions
- 13 December 1982
- journal article
- Published by Wiley in FEBS Letters
- Vol. 150 (1), 161-166
- https://doi.org/10.1016/0014-5793(82)81326-4
Abstract
CAMP-dependent protein kinase I and II (cAKI and cAKII) were incubated under near physiological conditions in the presence of various concentrations of 8-N3-c[3H]AMP or c[3H]AMP. Both types (A and B) of cyclic nucleotide binding sites of cAKI or cAKII were occupied to a similar extent and the degree of their occupation correlated with the degree of kinase activation. cAKI cAKII bound cAMP in an apparent positively cooperative manner in the presence of Mg2+, ATP. 8-N3-c[3H]AMP dissociated several orders of magnitude faster from site A than site B of the regulatory moeity of cAKII, and was photo-incorporated only when bound to site B.Keywords
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