Associative properties of the Escherichia coli galactose-binding protein and maltose-binding protein.
The ligand-binding characteristics of periplasmic galactose-binding protein and maltose-binding protein of Escherichia coli are analyzed. The saturation function was decreased upon increasing protein concentration and the monomer-dimer equilibrium was shifted towards the monomeric protein form upon an increase of the ligand concentration. An association constant K0 = 6 X 10(8) M-1 was found for the galactose-binding protein. These data fit a monomer-dimer system in equilibrium, in which the monomer has a higher affinity for the ligand.
D018528:ATP-Binding Cassette Transporters; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D005690:Galactose / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D008320:Maltose / Q000378:metabolism*; D058619:Maltose-Binding Proteins; D008433:Mathematics; D009004:Monosaccharide Transport Proteins; D033902:Periplasmic Binding Proteins
D018528:ATP-Binding Cassette Transporters; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D046911:Macromolecular Substances; C461619:MalE protein, E coli; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; D033902:Periplasmic Binding Proteins; C023550:galactose-binding protein; C461599:maltose transport system, E coli; D008320:Maltose; D005690:Galactose