אסיף מאגר המחקר החקלאי

Acetylcholine esterase as a probe for erythrocyte-membrane intactness

Year:

1974

Source of publication :

Authors :

Volume :

339

Co-Authors:

Aloni, B., Research and Development Authority, Department of Biology, University of the Negev, Beer Sheva, Israel
Livne, A., Research and Development Authority, Department of Biology, University of the Negev, Beer Sheva, Israel

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Abstract:

Erythrocyte acetylcholine esterase can be assayed in intact cells and was tested as a probe for membrane changes. Acetylcholine esterase activity correlated with the erythrocyte relative volume. Antihemolytic acyl sorbitols, fatty acids and phenothiazines inhibit to varying extents the activity of acetylcholine esterase. The inhibition of acetylcholine esterase by linolenoyl sorbitol was further characterized and found to be non-competitive and critically dependent on cell intactness over a wide temperature range. Neither solubilized nor ghost acetylcholine esterase was affected by the acyl sorbitol while under conditions optimal for ghost resealing, the enzyme resumed the sensitivity to the acyl sorbitol. Acetylcholine esterase sensitivity thus appears to be a promising tool to follow the dynamics of membrane integrity. © 1974.

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