[Mechanism of the phosphotransferase reaction catalyzed by guanosine-3',5'-monophosphate-dependent protein kinase].

The paper deals with the mechanism of the phosphotransferase reaction catalyzed by G-kinase purified from the shrimp tissue by affinity chromatography. The ATP functional groups are stated to be significant for interaction with the enzyme. A mathematical model of the reaction is suggested assuming two active centres in a G-kinase molecule.

[Affinity chromatography and properties of cGMP-dependent protein kinase from prawn tissues].

Using affinity chromatography on 8-(2-aminoethyl)-amino-cAMP Sepharose, the cGMP-dependent protein kinase (ATP: protein phosphotransferase, EC 2.7.1.

[Partial purification and properties of cGMP-dependent protein kinase from prawn tissue].

Using ion-exchange chromatography and gel filtration, cGMP-dependent protein kinase was purified from prawn tissues 220-fold with a yield of activity of 12%. The apparent Ka values for cGMP, cAMP and 8-Br-cGMP are 1 . 10(-7), 5 .