Abstract
1. 1. Creatine kinases were isolated from the ordinary muscle of red sea bream Pagrus major, Pacific mackerel Scomber japonicus and carp Cyprinus carpio by ammonium sulfate fractionation, followed by ion-exchange chromatography on CM-Sepharose CL-6B and DEAE-cellulose columns and gel filtration on a Sephacryl S-200 column, and examined for enzymatic properties. 2. 2. The creatine kinases showed the highest activity in a pH range from 7.0–7.5 in 30 mM Tris-histidine and 30 mM Tris-HCl buffers. K m values for creatine phosphate ranged from 2.0–10.6 mM and those for ADP from 0.20–0.33 mM. 3. 3. Fish muscle creatine kinases required Mg 2+ for activation as did rabbit enzyme. On the other hand, the fish enzymes were mostly or completely inactivated in the presence of 1 mM Zn 2+ or Co 2+, unlike rabbit enzyme which retained some activity. 4. 4. The enzymes of the two marine fishes were less thermostable than that of carp, even which was much more labile than rabbit enzyme.
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