The purification of coenzyme A by ion exchange chromatography.

With the increasing demand for coenzyme A (CoA) to be used as a substrate in enzyme studies, a need has developed for additional methods of isolating this substance from natural sources. Two methods have been published whereby CoA of reasonably high purity can be prepared (1, 2). Both of these procedures are lengthy and the over-all yields are relatively poor (10 to 30 per cent). One of these methods is relatively expensive, since large amounts of glutathione are required (2). In the present communication a method is described for the preparation of CoA of 50 to 65 per cent purity from crude yeast extract in fair yield (50 to 55 per cent) by a relatively simple two-step chromatographic procedure. In this procedure the CoA is adsorbed on charcoal and is concentrated by selective elution with ammoniacal acetone. The CoA concentrate thus obtained is adsorbed on a Dowex 1 resin and is isolated as a distinct fraction by elution with strong buffer. The final product contains 200 to 270 units (1) of CoA per mg.