Structure of membranes: reaction of red blood cell membranes with phospholipase C

Abstract

Treatment of human red blood cell membranes with phospholipase C releases 68 to 74 percent of the total membrane phosphorus into solution, through hydrolysis of membrane phospholipids to diglycerides and water-soluble phosphorylated amines. In spite of this drastic change, the membrane remains intact in phase microscopy, and the average protein conformation in the membranes, as determined by circular dichroism measurements in the ultraviolet, is unaffected. These results are readily explained by a model of membrane structure that is stabilized by hydrophobic interactions and in which the polar and ionic heads of lipids are on the outer surfaces of the membrane, in contact with the bulk aqueous phase and accessible to the action of phospholipase C.