Binding sites for horseradish peroxidase on the cell surface. Suppression of binding by gangliosides and effects of some bivalent cations.
The cytochemical reaction for surface-bound horseradish peroxidase (HRP) on cultured HeLa cells, GH3 cells, and isolated rat liver cells was suppressed by 30 microM monosialoganglioside, by 30 microM trisialoganglioside, or by 5 mM CMP-neuraminic acid. The reaction was also suppressed by 10 mM chitotriose or by 10 mM UDP-galactose, a galactose acceptor and donor, respectively, for galactosyl-transferase. The addition of 2 mM Mn2+ to the incubation medium with HRP suppressed the reaction for surface-bound HRP, and the addition of 10-20 mM Ca2+ intensified the reaction. The addition of 2 mM Zn2+ caused less inhibition than that of 2 mM Mn2+, and the addition of 2 mM Co2+ caused either a slight inhibition, or no inhibition. These observations support the hypothesis that HRP may be bound to a glycosyltransferase at the cell surface.
D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000494:pharmacology; D002413:Cations, Divalent / Q000494:pharmacology*; D002460:Cell Line; D003035:Cobalt / Q000494:pharmacology; D005732:Gangliosides / Q000494:pharmacology*; D006651:Histocytochemistry; D006735:Horseradish Peroxidase / Q000378:metabolism*; D008345:Manganese / Q000494:pharmacology; D008722:Methods; D010544:Peroxidases / Q000378:metabolism*; D051381:Rats; D014312:Trisaccharides / Q000494:pharmacology; D014531:Uridine Diphosphate Galactose / Q000494:pharmacology; D015032:Zinc / Q000494:pharmacology
D002413:Cations, Divalent; D005732:Gangliosides; D014312:Trisaccharides; D014531:Uridine Diphosphate Galactose; D003035:Cobalt; C041161:chitotriose; D008345:Manganese; D006735:Horseradish Peroxidase; D010544:Peroxidases; D015032:Zinc; D002118:Calcium