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.

Presence of horse blood group antigens in the major glycoprotein fraction of the erythrocyte membrane.

The aqueous phase of the chloroform/methanol extract of the horse erythrocyte membrane contained the blood group activities Ad, Dc or Dd. The factors Ad and Dc could be separated by gel filtration.