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Proton-linked L-fucose transport in Escherichia coli.

Authors
  • S A Bradley
  • C R Tinsley
  • J A Muiry
  • P J Henderson
Publication Date
Dec 01, 1987
Source
PMC
Keywords
Disciplines
  • Biology
  • Chemistry
  • Medicine
License
Unknown

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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