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Inhibition of Glyceraldehyde Phosphate Dehydrogenase by Salts other than Lithium Chloride

Biochemical Institute and the Department of Chemistry, the University of Texas, Austin

¹ National Science Foundation Predoctoral Fellow. Authors' address: The University of Texas, Austin, Texas, U.S.A.

Received for publication 18 August 1955.

SUMMARY

Lallier (1954) has shown that 0·4 M lithium chloride strongly inactivates glyceraldehyde phosphate dehydrogenase—a finding which might partially explain some of the developmental changes found in lithium-treated embryos. In an attempt to establish an enzymatic basis for the morphological effects of lithium ion on Hydra which have been observed in this laboratory (Ham & Eakin, 1955), we have repeated the enzyme study with lithium chloride and extended it to include a number of other salts as controls.

From typical data (Table 1), it is obvious that the inhibition of glyceraldehyde phosphate dehydrogenase activity is in no way a specific effect due to lithium ions. Both sodium chloride and potassium chloride produced a greater inhibition than did lithium chloride. From the various sodium salts tested, it was found that the anion may be of more importance than the cation in determining the degree of inhibition, although the cation also has some effect.

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