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L-arabinose binding protein from Escherichia coli B-r.

Authors
  • Hogg, R W
  • Englesberg, E
Type
Published Article
Journal
Journal of bacteriology
Publication Date
Oct 01, 1969
Volume
100
Issue
1
Pages
423–432
Identifiers
PMID: 4899002
Source
Medline
License
Unknown

Abstract

A protein which is capable of binding l-arabinose-1-(14)C has been isolated from l-arabinose-induced cultures of Escherichia coli B/r. Analysis for this l-arabinose-binding protein (ABP) in a number of l-arabinose-negative mutants suggests that the ABP is not coded for by any of the known genetic units of the l-arabinose complex yet is under the control of the regulator gene araC. The ABP has been purified and found to bind l-arabinose, d-fucose, d-xylose, and l-ribulose with decreasing affinities. The K(m) for l-arabinose is 5.7 x 10(-6)m. The molecular weight, as determined by equilibrium centrifugation, was found to be 32,000. The protein was observed to have many features that liken it to other recently isolated binding proteins that have been implicated in the active transport of small molecules.

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