Previous Article | Next Article ![]()
J Bacteriol. 1972 September; 111(3): 791-796
Copyright © 1972 American Society for Microbiology. All Rights Reserved.
1 Division of Biological and Medical Sciences, Brown University, Providence, Rhode Island 02912
ABSTRACT
A galactose-binding protein related to the mglP transport system of Escherichia coli increases its affinity and binding capacity for the substrate when exposed to both D-galactose and specific antibodies. For this increase to occur, the binding protein has to be in contact with D-galactose for at least 2 min prior to the addition of the antibodies. This reaction was used to show that other substrates of the mglP 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.
This article has been cited by other articles:
| Appl. Environ. Microbiol. | Infect. Immun. | Eukaryot. Cell |
|---|---|---|
| Mol. Cell. Biol. | J. Virol. | Microbiol. Mol. Biol. Rev. |
| ALL ASM JOURNALS |