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Journal of Lipid Research, Vol. 14, 152-159, March 1973
Copyright © 1973 by Lipid Research, Inc.

Kinetic dependence of phospholipase A₂ activity on the detergent Triton X-100

Edward A. Dennis

Department of Chemistry, University of California at San Diego, La Jolla, California 92037

A kinetic analysis is presented for the dependence of one form of phospholipase A₂ from cobra (Naja naja) venom on the presence of the nonionic detergent Triton X-100 for its activity towards egg phosphatidylcholine and synthetic dipalmitoyl glycerophosphorylcholine as substrates. An automatic recording pH-stat apparatus was employed in order to continuously monitor enzyme activity. The results obtained in this study are interpreted in terms of a change in the physical state of the phospholipid when Triton X-100 micelles convert phospholipid bilayers into mixed Triton X-100-phospholipid micelles; this is consistent with the requirement of this enzyme for substrates which are in micellar form rather than either monomers or bilayers. An apparent inhibition of phospholipase A₂ activity at high concentrations of Triton X-100 is described and discussed in terms of the micellar nature of the substrate.

Supplementary key words egg phosphatidylcholine • dipalmitoyl glycerophosphorylcholine • mixed micelles • phospholipid

Submitted on July 24, 1972
Accepted on October 30, 1972

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