Abstract
A lead‐sulfide method has been developed to produce zymograms of human red cell acid phosphatase. Two somewhat different zymograms were detected; the one was obtained with phenyl phosphate or [3‐naphthyl phosphate and the other with p‐nitrophenyl phosphate or phenolphthalein diphosphate as the substrate. On this basis it was suggested that these substrates could be classified into two groups: aromatic compounds with no substituent in addition to the ester group; and compounds with a substituent attached to the carbon at the para position relative to the ester group. The idea that the position of a substituent may be of importance for the catalytic activity of the red cell acid phosphatase was supported by the observation that o‐ and m‐nitrophenyl phosphate were only slowly hydrolyzed in contrast to p‐nitrophenyl phosphate.
Published Version
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