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3-Hydroxy-,3-methylgutaryl coenzyme A (HMG-CoA) reductase has been purified 200-fold from baker's yeast. Gel filtration using Sephadex G-200 and ultracentrifugation of the partially purified enzyme indicate an approximate molecular weight of 150,000-200,000. The enzyme is unstable in buffer solutions but is partially stabilized in the presence of mercaptoethanol.

Fructose-1,6-bisphosphate affects the rate of a large variety of enzyme reactions. In some instances its role as a physiologic effector is well documented. In many cases the effects of fructose bishosphate on particular enzymes have been demonstrated in vitro but the link to physiologic conditions has not yet been established. It is the purpose of this paper to summarize the scattered findings in fructose bisphosphate as an effector of enzyme reactions and to draw some conclusions about the role of the compound in metabolic regulation.

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