High density of transmembrane glycoproteins on the flagellar surface of boar sperm cells.
Membrane halves of boar sperm flagella were produced by freeze-fracture and labeled in situ with concanavalin A and wheat germ agglutinin; the lectins were visualized with protein-gold complexes. Concanavalin A and wheat germ agglutinin binding sites partition with both protoplasmic and exoplasmic halves of the membrane. A high density of lectin marking was found on protoplasmic membrane halves; we conclude that the label corresponds to transmembrane glycoproteins that, on freeze-fracture, are dragged across the outer (exoplasmic) half of the phospholipid bilayer. Our demonstration of numerous transmembrane proteins in sperm flagella offers the structural setting for previous models on flagellar surface motility that postulate accessibility of motile membrane components to the submembranous cytoskeleton.
D000818:Animals; D005407:Flagella / Q000648:ultrastructure*; D005614:Freeze Fracturing; D006023:Glycoproteins / Q000032:analysis*; D008051:Lipid Bilayers; D008297:Male; D008565:Membrane Proteins / Q000032:analysis*; D008854:Microscopy, Electron; D013094:Spermatozoa / Q000648:ultrastructure*; D013552:Swine
D006023:Glycoproteins; D008051:Lipid Bilayers; D008565:Membrane Proteins