Enzymic determination of acetaldehyde in blood

Abstract

The determination of acetaldehyde in blood by diffusion into semicarbazide is subject to interference from acetoacetate, which is partly decarboxylated to acetone during the procedure. A method is described based on the use of a K-requiring aldehyde dehydrogenase easily prepared from commercial dry yeast. The rate of formation of reduced diphosphopyridine nucleotide under standard conditions is proportional to the aldehyde concentration within a considerable range. Under the analytical conditions chosen a number of aldehydes will react; the specificity is therefore not complete. The accuracy of the method at very low aldehyde concentrations is better than that obtainable with other methods. The limit for detention of acetaldehyde in biological material is around 0.1 [mu]g/g.