Abstract
THERE has been much interest in identifying and characterizing the protein elements in cell membranes which seem to be involved in regulating membrane ionic permeability1–3. We now have further evidence that membrane-bound proteins in nerve axons are involved in ion permeability regulation. It was first found that external treatment of isolated crayfish nerve axons with the proteolytic enzymes papain, trypsin, and chymotrypsin (unpublished data) considerably affected the axons, resting permeability to potassium, sodium, and chloride, while having minimal effects on the action potential. It was also found that the external application of 1-fluoro 2,4-dinitrobenzene (which reacts with protein reactive groups) considerably reduced chloride permeability without reducing the resting membrane potential or action potential4.
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CLARK, H., STRICKHOLM, A. Evidence for a Conformational Change in Nerve Membrane with Depolarization. Nature 234, 470–471 (1971). https://doi.org/10.1038/234470a0
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DOI: https://doi.org/10.1038/234470a0
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