The catalytic subunit of cAMP-dependent protein kinase (EC 2.7.1.37) was purified for the first time from human placenta by DEAE-cellulose and HTP chromatography. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis showed a single band of average molecular weight of 42 kDa (SEM = 0.52). Kinetic experiments showed a Km for ATP of 12.6 ± 1.2 μmol/l, for histone II-AS of 1.3 ± 0.05 mg-ml^-1, for kemptide of 11.4 ±4.4 μmol/l. The synthetic inhibitor IP(20)-amide showed a competitive mechanism of inhibition with a K, of 5.0 nmol/1. The protein kinase inhibitors H7 and H9 showed an apparent K,of 8.3 and 4.9 μmol/1 respectively. Preparative isoelectric focusing revealed the presence of 5 different isoforms with an average pi of 6.17, 6.70, 7.15, 7.67, 8.9.

Keywords:
Adenosine 3':5'-monophosphate-dependent protein kinase, Placenta, Isoelectric focusing
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1991
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