Behavior of Acetyl Groups Combined with Sulfhydryl Groups in Protein

II. Behavior of Acetyl Groups Combined with Sulfhydryl Groups in Yeast Alcohol Dehydrogenase

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It was found that acetyl groups combined with SH groups in yeast alcohol dehydrogenase (YADH) were easily released and transferred to SH group of coenzyme A (CoA) in contrast with acetyl group bound to SH group of glutathione. Stabilization of thiolester bonds in S-acetyl-YADH was observed upon denaturation of the protein in the presence of urea.
These findings appeared to open new approach to a problem about mechanism of storage and supply of active acetyl groups in living cells.