Abstract
1. A method for purification and crystallization of L-glutamate dehydrogenase [EC 1.4.1.2–4] from rat kidney was described. 2. Various properties of the enzymes from rat liver and kidney were compared. Immunologically, the precipitin lines of the two enzymes fused completely with each other. No significant differences were found between the two enzymes with respect to their ultracentrifugal patterns, effect of purine nucleotides on it, electrophoretic behavior, pH optima, and Km values. Both enzymes did not polymerize as the enzyme concentration was raised, even in the presence of nucleotides. The enzymes of rat liver and kidney were identical in the protein nature. 3. The enzymes of rat liver and kidney responded differently to acidosis. The enzyme activity in the kidney was elevated in vivo on acidosis, but not in the liver. It was demonstrated by immunotitration that the increase in enzyme activity in the kidney was due to the increase in the enzyme protein content.
Published Version
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