The concentration of acetate in most mam- malian blood and tissues is extremely low and quantitative determination has not been possible with the methods used, for instance, in micro- biology. Various suggestions have been made to employ enzymic procedures for the quantitative analysis of acetate. Korff (1954) examined the combination of the distillation-diffusion step described by Bartley ( The enzymic reactions involved were activation of acetate to acetyl-coenzyme A and condensation of this sub- stance with oxaloacetate, produced through de- hydrogenation of malate. This last reaction caused the formation of reduced diphosphopyridine nucleotide, which was measured spectrophotometrically. The enzyme preparation was a rather crude one and contained lactic dehydrogenase, which causes pyruvate to interfere in the determination. Sodium ions inhibit the process strongly and the enzyme is not stable for long periods. Korff's method was designed to measure 3-25 ,g. of acetate. Rose (1955) has utilized an acetokinase from Escherichia coli. The acetyl phosphate formed in the reaction was measured as the ferric hydroxamate complex. Amounts of acetate in the range 30-150 ,g. were determined.
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Lundquist et al. (1961) studied this question.
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