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1. The phosphatidylcholine-cholesterol acyltransferase of rat plasma was dissociated from the plasma lipoproteins by ultracentrifugation and shown to be present in the plasma residual-protein fraction of density &gt;1.210. 2. The general properties of the acyltransferase were substantially unchanged in the residual fraction as judged from the effects of differences in the substrates and of overnight starvation on the formation of different cholesterol esters. 3. The enzyme from rats starved overnight, by comparison with the enzyme from fed rats, preferentially formed cholesteryl arachidonate at the expense of cholesteryl linoleate. 4. The results suggest that ultracentrifugal separation of the plasma residual fraction may be used as an initial step for the purification of the acyltransferase.

Phosphatidylcholine–cholesterol acyltransferase in the ultracentrifugal residual protein fraction of rat plasma