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Abstract
The effect of palytoxin was studied in a microsomal fraction enriched in longitudinal tubules of the sarcoplasmic reticulum membrane. Half-maximal effect of palytoxin on Ca 2+-ATPase activity yielded an apparent inhibition constant of approx. 0.4 μM. The inhibition process exhibited the following characteristics: (i) the degree of inhibition was dependent on membrane protein concentration; (ii) no protection was observed when the ATP concentration was raised; (iii) dependence on Ca 2+ concentration with a decreased maximum catalytic rate; (iv) it occurred in the absence of Ca 2+ ionophoric activity. Likewise, the inhibition mechanism was linked to: (i) rapid enzyme phosphorylation from ATP in the presence of Ca 2+ but lower steady-state levels of phosphoenzyme; (ii) more drastic effect on phosphoenzyme levels when the toxin was added to the enzyme in the absence of Ca 2+; (iii) decreased phosphoenzyme levels at saturating Ca 2+ concentrations; (iv) no effect on kinetics of phosphoenzyme decomposition. The palytoxin effect is related with lock of the enzyme in the Ca 2+-free conformation so that progression of the catalytic cycle is impeded.
Published Version
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