The binding of maltose to 'virgin' maltose-binding protein is biphasic.
The biphasic binding properties of the galactose-binding and maltose-binding proteins of Escherichia coli may be important in the functioning of these proteins as recognition components of chemoreceptors. However, Richarme and Kepes [Eur. J. Binding curve of the galactose-binding protein may be the result of isotopic dilution, during equilibrium dialysis, by unlabeled ligand retained by the binding throughout purification. Here the binding of maltose to maltose-binding protein which has never previously been exposed to sugar ('virgin' binding protein) is shown to be biphasic. This implies that the unusual binding properties are attributable to the maltose-binding protein itself.
D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism; D001665:Binding Sites; D002633:Chemotaxis; D004926:Escherichia coli / Q000378:metabolism; D005690:Galactose / Q000378:metabolism; D005990:Glycerol / Q000378:metabolism; D007700:Kinetics; D008320:Maltose / Q000378:metabolism; D011485:Protein Binding; D011955:Receptors, Drug
D001426:Bacterial Proteins; D011955:Receptors, Drug; D008320:Maltose; D005990:Glycerol; D005690:Galactose