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W A Hamilton

Publications and source records attributed to W A Hamilton.

At least 37 records · Page 2Linked to original sources
PubMed1980

Quantitative analysis of proton-linked transport system. beta-Galactoside exit in Escherichia coli.

The exit of lactose and thiomethyl-beta-D-galactoside from Escherichia coli ML308-225 has been studied to determine the role of carrier-dependent (zero-trans efflux) and carrier-independent (leak) processes. On the basis of its sensitivity to p-chloromercuribenzene sulphonate the exit of lactose was found to be almost wholly mediated by the carrier. Consistent with this conclusion was the finding that the rate of exit of this sugar was dependent on the external pH, being considerably slower at acid pH. On the other hand exit of thiomethyl-beta-D-galactoside was found to be composed of both carrier-dependent and carrier-independent processes. Both processes exhibited first-order kinetics with the rate constants for zero-trans efflux and leak being 0.137 min-1 and 0.079 min-1, respectively. The relevance of these findings for out earlier proposal for the methods of attenuation of solute accumulation is discussed [Booth, Mitchell & Hamilton (1979) Biochem. J. 182, 687--696].

4-Chloromercuribenzenesulfonate↗
PubMed1980

Two views on philanthropy: what does the future hold.

What is the philanthropic outlook for the 1980's? Will giving be consistent with the decline of the dollar? How can non-profits deal with the skyrocketing costs of management and fund raising? These issues are surveyed in separate points of view from two leading philanthropic experts, drawn from their years of experience in the non-profit sector.

Age Factors↗
PubMed1979

Quantitative analysis of proton-linked transport systems. Glutamate transport in Staphylococcus aureus.

1. The magnitude of the protonmotive force in respiring Staphylococcus aureus was measured over the range of extracellular pH from 5.6 to 7.8. 2. The membrane potential remains constant at 150 mV, inside-negative, but the pH gradient decreases from 2.1 units, inside-alkaline, at pH 5.6 to zero at pH 7.5 and above. 3. The accumulation of glutamate in the soluble cell pool is pH-independent at a value equivalent to 100 mV. 4. The results of experiments studying co-transport of protons are consistent with a proton/glutamate stoichiometry of 2 and electrogenic transport across the pH range examined. 5. The amount of glutamate uptake is the result of a kinetic steady state between influx and efflux pathways. 6. Evidence is presented for the regulation of this kinetic steady state by the response of the initial rate of uptake to changes in the protonmotive force.

Biological Transport↗
PubMed1979

Quantitative analysis of proton-linked transport systems. The lactose permease of Escherichia coli.

Evidence is presented that lactose uptake into whole cells of Escherichia coli occurs by symport with a single proton over the range of external pH 6.5--7.7. The proton/lactose stoicheiometry has been measured directly over this pH range by comparison of the initial rates of proton and lactose uptake into anaerobic resting cell suspensions of E. coli ML308. Further, the relationship between the protonmotive force and lactose accumulation has been studied in E. coli ML308-225 over the range of external pH 5.9--8.7. At no point was the accumulation of the beta-galactoside in thermodynamic equilibrium with the protonmotive force. It is concluded that the concentration of lactose within the cell is governed by kinetic factors rather than pH-dependent changes in the proton/substrate stoicheiometry. The relevance of these findings to the model of pH-dependent proton/substrate stoicheiometries derived from studies with E. coli membrane vesicles is discussed.

Biological Transport↗
PubMed1976

Magnitude of the protonmotive force in respiring Staphylococcus aureus and Escherichia coli.

The membrane potential and pH gradient developed across the plasma membranes of whole cells of Staphylococcus aureus and spheroplasts of Escherichia coli were estimated. The distributions of potassium ions in the presence of valinomycin and the pH gradient across the membrane were determined from the changes in pK and pH observed in the external medium during transition from the energized respiring state to the de-engerized resting condition. The protonmotive force in respiring cells was estimated at 211 mV for S. aureus and 230 mV for E. coli at external pH values of approximately 6.5. The adequacy of these protonmotive forces as a driving force for substrate accumulation or adenosine 5'-triphosphate synthesis is discussed.

Adenosine Triphosphate↗
PubMed1976

Proton movements coupled to lactate and alanine transport in Escherichia coli: isolation of mutants with altered stoichiometry in alanine transport.

The addition of lactate to lightly buffered suspensions of resting cells of Escherichia coli caused an increase in the pH of the extracellular phase as lactate and protons entered the cell together. From the magnitude of the pH change and the non-electrogenic character of lactate uptake, we concluded that the stoichiometry of the process was 1 proton/lactate anion. The addition of alanine caused a slow increase in pH, also apparently due to the transport of the amino acid by a symport mechanism with 1 proton/alanine stoichiometry. When cells were grown in the chemostat with alanine as sole carbon source and as limiting nutrient, this stoichiometry was found to alter to 2 protons/alanine, and then to 4 protons/alanine. These increases stoichiometries were due to the selection of mutants. The consequences of these changes on the potential uptake capacity of the cells are discussed.

Alanine↗