The lectin-binding sites of the erythrocyte membrane components of horse, swine and sheep. Characterization by their molecular weights.
The membrane components of equine, porcine and ovine erythrocytes were separated by sodium dodecylsulfate polyacrylamide gel electrophoresis and subsequently incubated with the radioiodinated lectins from lentils (LCH), castorbeans (RCA), Phaseolus beans (L-PHA), gorse seeds (UEH-F) and from vineyard snails (HPA). The following individual glycoproteins could be labeled: gp 26, 33, 100 and 320 in horse erythrocytes, gp 24, 46, 75, 130 and 210 in swine and gp 24, 57, 100 and 210 in sheep erythrocytes.
D000818:Animals; D004910:Erythrocyte Membrane / Q000648:ultrastructure*; D004912:Erythrocytes / Q000648:ultrastructure*; D006384:Hemagglutination; D006736:Horses; D006801:Humans; D037102:Lectins; D008565:Membrane Proteins / Q000097:blood*; D008970:Molecular Weight; D012756:Sheep; D013045:Species Specificity; D013552:Swine
D037102:Lectins; D008565:Membrane Proteins