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Methods in Enzymology | 1986

Anion exchange in bacteria: reconstitution of phosphate: hexose 6-phosphate antiport from Streptococcus lactis.

Suresh V. Ambudkar; Peter C. Maloney

Publisher Summary This chapter discusses methods for measuring protonmotive force (PMF) and the motility that is the consequence of its use. The best-studied type of bacterial motility derives from the use of external flagella. The external flagellar filaments are thin helical structures that themselves perform no transduction of metabolic energy into mechanical work. They are rotated by motors at their base, and their rotation generates thrust. The motors are reversible, and it is this that permits control of behavior, as the reversal probability is controlled by the environment. It should be noted that PMF can, under some circumstances at least, play a role in controlling the “switching” of the flageilar motor. Major examples of this are aerotaxis and phototaxis, which appear to be more strictly “PMF taxis.” Another related aspect is pH taxis and certain classes of repellent-induced taxes, where perturbation of either internal or external pH is responsible for affecting motor switching.


Microbiological Research | 1990

Anion-exchange mechanisms in bacteria.

P C Maloney; Suresh V. Ambudkar; V Anatharam; L A Sonna; A Varadhachary


Journal of Biological Chemistry | 1992

Identification, purification, and reconstitution of OxlT, the oxalate: formate antiport protein of Oxalobacter formigenes.

Zhong Shi Ruan; Vellareddy Anantharam; Isabelle T. Crawford; Suresh V. Ambudkar; Seung Y. Rhee; Milton J. Allison; Peter C. Maloney


Journal of Biological Chemistry | 1986

Reconstitution of sugar phosphate transport systems of Escherichia coli.

Suresh V. Ambudkar; T J Larson; P C Maloney


Journal of Biological Chemistry | 1986

Bacterial anion exchange. Use of osmolytes during solubilization and reconstitution of phosphate-linked antiport from Streptococcus lactis.

Suresh V. Ambudkar; Peter C. Maloney


Journal of Biological Chemistry | 1988

The mechanism of glucose 6-phosphate transport by Escherichia coli.

L A Sonna; Suresh V. Ambudkar; Peter C. Maloney


Journal of Biological Chemistry | 1990

UhpT, the sugar phosphate antiporter of Escherichia coli, functions as a monomer.

Suresh V. Ambudkar; Vellareddy Anantharam; Peter C. Maloney


Journal of Biological Chemistry | 1986

Reconstitution of ATP-dependent calcium transport from streptococci

Suresh V. Ambudkar; A R Lynn; P C Maloney; B P Rosen


Journal of Biological Chemistry | 1984

Characterization of Phosphate:Hexose 6-Phosphate Antiport in Membrane Vesicles of Streptococcus lactis"

Suresh V. Ambudkar; Peter C. Maloney


Proceedings of the National Academy of Sciences of the United States of America | 1986

Variable stoichiometry of phosphate-linked anion exchange in Streptococcus lactis: implications for the mechanism of sugar phosphate transport by bacteria

Suresh V. Ambudkar; Larry A. Sonna; Peter C. Maloney

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Peter C. Maloney

Johns Hopkins University School of Medicine

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L A Sonna

Johns Hopkins University

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A R Lynn

Johns Hopkins University

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A Varadhachary

Johns Hopkins University

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B P Rosen

Johns Hopkins University

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Larry A. Sonna

Johns Hopkins University

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M P D'Souza

Johns Hopkins University

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T J Larson

Johns Hopkins University

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V Anatharam

Johns Hopkins University

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