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EFFECTS OF TRITON X-100 UPON THE ACTIVITY OF SOME ELECTROPHORETICALLY SEPARATED ACID PHOSPHATASES AND ESTERASES

SALLY LYMAN ALLEN 1, JOHN M. ALLEN 1, and BARBARA MORRISON LICHT 1

1 Department of Zoology, The University, of Michigan, Ann Arbor, Michigan

Triton X-100, a non-ionic detergent, was incorporated into reaction mixtures used for the visualization of esterases and acid phosphatases separated by electrophoresis in starch gels. Its effects were tested, in combination with 12 different substrates, on enzymes derived from Tetrahymena pyriformis and rat liver. The effects of Triton X-100 were complex. It promoted the solubilization of some substrates, notably the agr-naphthyl fatty acid esters. It also altered the color of the enzymatically produced end product. The net effect was apparent enhancement of enzymatic activity with certain substrates and apparent inhibition of enzymatic activity with other substrates. Differential activation and inhibition of some of the electrophoretically resolved enzymes was observed. Both quantitative and electrophoretic studies indicated that Triton X-100 is an activator of certain esterases. A cathodally migrating acid phosphatase of rat liver was activated by Triton X-100 in the presence of naphthol AS, naphthol AS-BI, or naphthol AS-MX phosphates.

Submitted on December 28, 1964


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