Interactions of hexachlorocyclohexanes with the (Ca2+ + Mg2+)-ATPase from sarcoplasmic reticulum

O. T. Jones, R. J. Froud, A. G. Lee

    Research output: Contribution to journalArticlepeer-review


    Hexachlorocyclohexanes have been shown to inhibit the (Ca2+ + Mg2+)-ATPase of muscle sarcoplasmic reticulum reconstituted into bilayers of dioleoylphosphatidylcholine. However, for the ATPase reconstituted into bilayers of dimyristoleoylphosphatidylcholine, a pattern of activation at low concentration followed by inhibition at higher concentration is seen for hexachlorocyclohexanes and alkanes such as decane and hexadecane. The ATPase in sarcoplasmic reticulum vesicles is also inhibited by the hexachlorocyclohexanes. The effects of hexachlorocyclohexanes on activity are largely independent of concentrations of Ca2+ and ATP. Inhibition is more marked at lower temperatures. The hexachlorocyclohexanes quench the tryptophan fluorescence of the ATPase, and the quenching can be used to obtain partition coefficients into the membrane system. As for simple lipid bilayers, partition exhibits a negative temperature coefficient. Binding is related to effects on ATPase activity. © 1985.
    Original languageEnglish
    Pages (from-to)740-751
    Number of pages11
    JournalBiochimica et Biophysica Acta - Biomembranes
    Issue number3
    Publication statusPublished - 14 Feb 1985


    • (Ca2+ + Mg2+)-ATPase
    • (Rabbit skeletal muscle)
    • Hexachlorocyclohexane
    • Insecticide-membrane interaction
    • Lindane
    • Sarcoplasmic reticulum


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