Compartmentalization of intracellular membrane glycocomponents is revealed by fracture-label.
We used thin-section fracture-label to determine the distribution of wheat-germ agglutinin binding sites in intracellular membranes of secretory and nonsecretory rat tissues as well as in human leukocytes. In all cases, analysis of the distribution of wheat germ agglutinin led to the definition of two endomembrane compartments: one, characterized by absence of the label, includes the membranes of mitochondria and peroxisomes as well as those of the endoplasmic reticulum and nuclear envelope; the other, strongly labeled, comprises the membrane of lysosomes, phagocytic vacuoles, and secretory granules, as well as the plasma membrane. The Golgi apparatus was weakly labeled in all studied tissues.
D000818:Animals; D002451:Cell Compartmentation; D003208:Concanavalin A; D005614:Freeze Fracturing; D006017:Glycolipids / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D006056:Golgi Apparatus / Q000648:ultrastructure; D007425:Intracellular Membranes / Q000648:ultrastructure*; D037102:Lectins; D008247:Lysosomes / Q000648:ultrastructure; D008830:Microbodies / Q000648:ultrastructure; D008854:Microscopy, Electron; D008928:Mitochondria / Q000648:ultrastructure; D051381:Rats; D014909:Wheat Germ Agglutinins
D006017:Glycolipids; D006023:Glycoproteins; D037102:Lectins; D014909:Wheat Germ Agglutinins; D003208:Concanavalin A