The ‘compartmentation’ of choline acetyltransferase within the synaptosome

Abstract

Choline acetyltransferase may be isolated in either a bound or soluble form after hypo-osmotic treatment of a crude synaptosome fraction, depending on the conditions. In the bound form, the enzyme appears to be associated with the larger membrane fragments rather than with synaptic vesicles. The bound form is predominant at slightly acid pH values and low ionic strength, the soluble form under more physiological conditions of pH and ionic strength. Sodium chloride, potassium chloride, magnesium chloride and calcium chloride at similar ionic strengths solubilize the enzyme. Choline acetyltransferase was found to be soluble under these conditions after release from synaptosomes from rat and pigeon cerebra, guinea-pig cortex and rabbit cortex, caudate nuclei, diencephalon and midbrain. Certain isoenzymes of lactate dehydrogenase behaved similarly.