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Journal of Pharmacology And Experimental Therapeutics, Vol. 96, Issue 2, 114-118, 1949
Copyright © 1949 by American Society for Pharmacology and Experimental Therapeutics

THE INHIBITION OF ACID PHOSPHATASE OF SHEEP BRAIN

ALBERT M. MATTOCKS 1 and SALLY D. HOLTAN 1

1 School of Pharmacy, Western Reserve University, Cleveland, Ohio

1. Structural similarity between certain drugs known to act on the nervous system and glycerophosphorylcholine suggested possible competitive action, and a number of these drugs were tested for their effect on the hydrolysis of betaglycerophosphate and phosphorylcholine by brain extracts at pH 5.0. Only one of the drugs tested (DFP) inhibited the enzyme system, and it was concluded that acid phosphatases are not the site of action of these substances.

2. Fluoride inhibited noncompetitively; sulfate, pyrophosphate, and DFP inhibited acid glycerophosphatase competitively, their Ki values being 7.52 x 10-4, 2.35 x 10-4, and 5.04 x 10-4, respectively.

Submitted on January 17, 1949






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