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. 1987 Dec 1;248(2):495-500.
doi: 10.1042/bj2480495.

Proton-linked L-fucose transport in Escherichia coli

S A Bradley  1 , C R Tinsley, J A Muiry, P J Henderson
Affiliations

Proton-linked L-fucose transport in Escherichia coli

S A Bradley et al. Biochem J. .

Abstract

1. Addition of L-fucose to energy-depleted anaerobic suspensions of Escherichia coli elicited an uncoupler-sensitive alkaline pH change diagnostic of L-fucose/H+ symport activity. 2. L-Galactose or D-arabinose were also substrates, but not inducers, for the L-fucose/H+ symporter. 3. L-Fucose transport into subcellular vesicles was dependent upon respiration, displayed a pH optimum of about 5.5, and was inhibited by protonophores and ionophores. 4. These results showed that L-fucose transport into E. coli was energized by the transmembrane electrochemical gradient of protons. 5. Neither steady state kinetic measurements nor assays of L-fucose binding to periplasmic proteins revealed the existence of a second L-fucose transport system.

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References

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