Nature of the interaction between Ricinus communis agglutinin and blood cells.
Binding of Ricinus communis agglutinin (RCA 120) to carbohydrate receptors of human lymphocytes and erythrocytes is enthalpically driven. As in the case of simple saccharides, the delta S contribution is always unfavorable to the interaction. This result is different from that observed for other lectins and might indicate that hydrophobic interactions do not play a dominant role in binding of RCA 120 to cell surfaces.
D000017:ABO Blood-Group System; D000089:Acetic Anhydrides; D002250:Carbon Radioisotopes; D002367:Ricinus communis; D004912:Erythrocytes / Q000276:immunology*; D005690:Galactose; D006801:Humans; D007700:Kinetics; D007785:Lactose; D037102:Lectins; D008214:Lymphocytes / Q000276:immunology; D037121:Plant Lectins; D010940:Plant Proteins; D010947:Plants, Toxic; D011975:Receptors, Mitogen / Q000032:analysis; D012278:Ricinus; D013816:Thermodynamics
D000017:ABO Blood-Group System; D000089:Acetic Anhydrides; D002250:Carbon Radioisotopes; D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins; D011975:Receptors, Mitogen; C017707:Ricinus communis agglutinin-1; C032650:Ricinus communis lectin receptor; C031800:acetic anhydride; D007785:Lactose; D005690:Galactose