A major 125-kd membrane glycoprotein of @entity375 is attached to the lipid bilayer through an XXXX -containing phospholipid.

@entity1 @entity844 @entity8580 @entity3177 @entity2915 @entity375 @entity4357
A number of plasma membrane glycoproteins of @entity1 and protozoan origin are released from cells by @entity4357 -specific phospholipase C. Some of these proteins have been shown to be attached to the lipid bilayer via a covalently linked, structurally complex glycophospholipid. Here we establish the existence of similarly linked glycoproteins in the @entity375 @entity375 . The most abundant of these is a tightly membrane-bound glycoprotein of 125 kd. The detergent-binding moiety of this protein can be removed by @entity4357 -specific phospholipase C of bacterial origin or from @entity3177 . Metabolic labeling indicates that the protein contains covalently attached @entity844 and @entity8580 . It also contains the @entity2915 ( @entity2915 ), an antigen found previously on the glycophospholipid anchor of protozoan and @entity1 origin. Treatment of the protein with endoglycosidases F and H results in a 95-kd species. In the secretion mutant sec18, grown at 37 degrees C, the vesicular transport of glycoproteins is reversibly blocked between the rough endoplasmic reticulum and the Golgi apparatus. We find that sec18 cells, when grown at 37 degrees C, do add phospholipid anchors to newly synthesized glycoproteins. This indicates that these anchors are added in the rough endoplasmic reticulum.
