Antibody-Mediated Modification of the Binding Properties of a Protein Related to Galactose Transport
Author(s) -
Boris Rotman,
J. Hugh Ellis
Publication year - 1972
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.111.3.791-796.1972
Subject(s) - galactose , biology , antibody , biochemistry , plasma protein binding , escherichia coli , binding site , substrate (aquarium) , binding protein , transport protein , biophysics , immunology , ecology , gene
A galactose-binding protein related to themglP transport system ofEscherichia coli increases its affinity and binding capacity for the substrate when exposed to bothd -galactose and specific antibodies. For this increase to occur, the binding protein has to be in contact withd -galactose for at least 2 min prior to the addition of the antibodies. This reaction was used to show that other substrates of themglP transport system compete with galactose for a site(s) of the binding protein and that the degree of competition is comparable to that observed in vivo. A model for substrate translocation is presented postulating a cellular component that can induce conformational changes in the galactose-binding protein similar to those caused by antibodies.
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