AbstractAmong lectins fromLotus tetragonolobus, Ulex europaeus IandEvonymus europaea, agglutinating cells with blood group H determinants containingL‐fucose α1→2‐linked to subterminalD‐galactose, only the last lectin agglutinates thioglycolate‐ and paraffin oil‐stimulated murine and guinea pig peritoneal exudate cells (PEC). The agglutination is inhibited by specific inhibitors of Evonymus lectin only: lacto‐N‐fucopentaose I and lactose. These results suggest the presence of a determinant on the surface of PEC, containingL‐fucose α1‐linked at the nonreducing end which is different from blood group H determinants. Nonstimulated murine peritoneal cells (PC) are not agglutinated by the lectin but become agglutinable after neuraminidase treatment. Unstimulated guinea pig PC from different animals are agglutinated to a different extent by the same lectin concentration and show increased agglutinability after neuraminidase digestion. These results show that receptor for Evonymus lectin also exists on the nonstimulated PC but access to it is hindered by sialic acid. Trypsin‐ and pronase‐digested PEC show increased agglutinability with Evonymus lectin. These results suggest that the lectin receptor is a glycolipid.Since α‐linkedL‐fucose has been suggested as a part of the macrophage receptor for migration inhibitory factor in the guinea pig (Remold,J. Exp. Med.1973.138: 1065), the effect ofEvonymus europaealectin on the migration of PEC was studied. It was found that lectin inhibits the migration of PEC in the