Behavior of acetyl groups combined with sulfhydryl groups in protein. II. Behavior of acetyl groups combined with sulfhydryl groups in yeast alcohol dehydrogenase.

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 gluta thione. 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 mecha nism of storage and supply of active acetyl groups in living cells .