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Two-dimensional gel electrophoresis and Western blotting were used to analyze the kinase and phosphatase activity of the protein phosphorylation system in the skeletal muscle of the catfish (Clarias gariepinus). A minimum set of protein substrates and phosphorylated residues were selected to ascertain that the phosphorylation system was generally active in the fish and to gain insight into the differential regulation of phosphorylation in different parts of the muscle. The activation of protein phosphorylation was found to occur during hypoxia in the muscle cells of catfish and during anoxia in the fish at rest. An increase of protein phosphorylation was also observed after a single high-intensity exercise. This activation was transient, with a kinetics similar to the changes in the activity of glycogen phosphorylase a and b. The transient nature of the phosphorylation that was observed in the fish at rest suggests that it is a physiological response of the