Interaction of alpha-agglutinin with Saccharomyces cerevisiae a cells.
Binding of Saccharomyces cerevisiae alpha-agglutinin to target a cells was assayed by agglutination inhibition and 125I-alpha-agglutinin binding. The assays showed characteristics of equilibrium binding, namely saturability, competability, and the establishment of a kinetic endpoint in the presence of free alpha-agglutinin and free receptor. The binding was heterogeneous, displaying strong binding (10(9) liters/mol) and a weaker interaction. There were about 2 X 10(4) strong binding sites per a cell. Denaturing gels displayed identical labeled species binding to the a cells in the weak and strong interactions. Furthermore, weakly bound material could subsequently bind tightly to fresh a cells, implying that the same species of alpha-agglutinin was bound in the two states.
D000371:Agglutination; D000373:Agglutinins / Q000378:metabolism*; D001665:Binding Sites; D005656:Fungal Proteins / Q000378:metabolism*; D007457:Iodine Radioisotopes; D007700:Kinetics; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D013816:Thermodynamics
D000373:Agglutinins; D005656:Fungal Proteins; D007457:Iodine Radioisotopes