An investigation into the feasibility of using azide-insensitive ATPase and ConA as yeast plasma membrane markers.
Cytochemical localization of Concanavalin A binding sites in protoplasts of Candida tropicalis, investigated with glycosylated-ferritin and electron microscopy, showed that the lectin was specifically bound to the external protoplast surface. Thus, the plasma membranes have been labelled with 125I-Concanavalin A and followed through the isolation procedure. Relative distribution of 125I-radioactivity and azide-insensitive ATPase activity in the obtained fractions, suggested that this enzyme was an equivocal plasma membrane marker. Despite the presence of internal Concanavalin A binding sites, Concanavalin A could be used unambiguously as an exogenous plasma membrane marker of intact protoplasts.
D000251:Adenosine Triphosphatases / Q000032:analysis*; D001386:Azides / Q000494:pharmacology; D001665:Binding Sites; D017301:Ca(2+) Mg(2+)-ATPase; D002175:Candida / Q000378:metabolism / Q000648:ultrastructure*; D002462:Cell Membrane / Q000032:analysis* / Q000378:metabolism; D003208:Concanavalin A / Q000378:metabolism*; D006651:Histocytochemistry; D011523:Protoplasts / Q000378:metabolism
D001386:Azides; D003208:Concanavalin A; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase