Acetyl Coenzyme A

Add time:08/23/2019    Source:sciencedirect.com

Publisher SummaryThis chapter describes a method for the enzymatic determination of acetyl coenzyme A. The best method for the determination of acetyl-CoA makes use of enzymatic acetylation of aromatic amines. This has the following advantages over other methods: the difference in free energy for the hydrolysis of the acylmercaptan and the carbon-amide bond is at least 4 kcal/mole and guarantees a quantitative conversion; with a suitable acceptor the reaction can be followed spectrophotometrically; the method for the purification of arylamine transacetylase is easily reproducible and requires little expenditure of time and material. Initially, sulphanilamide or p-aminobenzoic acid were used as acceptor amines, then later, p-aminobenzene-sulphonic acid and aminoazobenzene; the most suitable is p-nitroaniline. Even in a deep-freeze the enzyme solutions have a limited stability. Solutions of acetyl-CoA are stable in the cold between pH 4 and 6. In alkaline solution a rapid hydrolysis occurs and even in strongly acid solution, there is a gradual decrease of activity. Neutral solutions of thioglycollate are extremely rapidly autoxidized. The acid solution should be stored in a deep freeze but must not be used for longer than 10 to 15 days.

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