title: Hydrophobicity of lectins. I. The hydrophobic character of concanavalin A.
abstract: The hydrophobicity of Concanavalin A has been estimated by its tendency to adsorb to hydrophobic adsorbents. Experiments varying temperature, salt concentration and hydrophobicity of the absorbent were consistent with accepted criteria of hydrophobic interaction between biomolecules and hydrophobic ligands. The biological significance of the hydrophobic character of Concanavalin A is also discussed.
mesh_terms: D000327:Adsorption; D055598:Chemical Phenomena; D002621:Chemistry; D003208:Concanavalin A; D007457:Iodine Radioisotopes; D007553:Isotope Labeling; D037102:Lectins; D011487:Protein Conformation; D013696:Temperature
chemical_list: D007457:Iodine Radioisotopes; D037102:Lectins; D003208:Concanavalin A