Abstract
A study was made of the action of phosphatidase D (phospholipase D) from Clostridium perfringens (C. welchii) on five constituents of the yolk of hens' eggs (α- and β-lipovitellin, the low-density lipoprotein fraction, granules, and lecithin) in aqueous solution, in the absence and presence of chloroform. Although the untreated lipovitellins were little affected by the enzyme, after absorption of chloroform, a large proportion of their phospholipids was hydrolyzed. In this respect they resembled lecithin but differed from the low-density yolk lipoproteins, whose phospholipids were rapidly hydrolyzed by the enzyme in the presence or absence of chloroform. The mechanism of this type of chloroform activation is discussed.
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