Open AccessThe Binding of Maltose to ‘Virgin’ Maltose‐Binding Protein is Biphasic
Author(s) -
HAZELBAUER Gerald L.
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb21022.x
Subject(s) - maltose binding protein , maltose , biochemistry , galactose , chemistry , binding site , binding protein , plasma protein binding , escherichia coli , sucrose , recombinant dna , fusion protein , gene
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. Biochem. 45, 127‐133 (1974)] have suggested that the biphasic 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 the sugar (‘virgin’ binding protein) is shown to be biphasic. This implies that the unusual binding properties are attributable to the maltose‐binding protein itself.