Abstract

Beef liver and beef spinal cord d-glycerate dehydrogenases have been shown to be extremely similar. No differences between the two enzymes could be shown by polyacrylamide electrophoresis, sodium dodecyl sulfate polyacrylamide electrophoresis, immunodiffusion, immunoelectrophoresis, or their response to certain inhibitors. Differences could be obtained, however, between the beef spinal cord enzyme and the hog spinal cord enzyme by immunodiffusion and immunoelectrophoresis. Only by the very sensitive technique of microcomplement fixation could a small but significant difference be shown between the beef liver and beef spinal cord enzymes. Like the beef liver and hog spinal cord enzymes, the beef spinal cord enzyme was not inhibited by high concentrations of serine or glycine. The enzyme was inhibited however by low concentrations of phosphohydroxypyruvate and by other phosphorylated compounds.

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