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Biomedical subjects

T H Wilson

Publications and source records attributed to T H Wilson.

At least 127 records · Page 7Linked to original sources
PubMed1976

Penetrating trauma of colon, cava, and cord.

A case is presented of a young police officer shot in the abdomen, sustaining injuries to colon, cava, and cord. Each injury was surgically managed in what was felt to be an appropriate manner, with early antibiotic therapy. As complications developed, aggressive measures were taken to correct them, with some success as far as pulmonary and renal failure were concerned, but with complete inability to reverse the meningitis and cerebritis caused by E. coli, and leading to a fatal outcome.

Abdominal Injuries↗
PubMed1976

Protonmotive force as the source of energy for adenosine 5'-triphosphate synthesis in Escherichia coli.

Net synthesis of adenosine 5'-triphosphate (ATP) in energy-depleted cells of Escherichia coli was observed when an inwardly directed protonmotive force was artificially imposed. In wild-type cells, ATP synthesis occurred whether the protonmotive force was dominated by the membrane potential (negative inside) or the pH gradient (alkaline inside). Formation of ATP did not occur unless the protonmotive force exceeded a value of 200 mV. Under these conditions, no ATP synthesis was found when cells were exposed to an inhibitor of the membrane-bound Ca2+- and Mg2+- stimulated adenosine triphosphatase (EC 3.6.1.3), dicyclohexylcarbodiimide, or to a proton conductor, carbonylcyanide-p-trifluoromethoxyphenyl-hydrazone. Adenosine triphosphatase-negative mutants failed to show ATP synthesis in response to either a membrane potential or a pH gradient. ATP synthesis driven by a protonmotive force was observed in a cytochrome-deficient mutant. These observations are consistent with the chemiosmotic hypothesis of Mitchell (1961, 1966, 1974).

Adenosine Triphosphatases↗
PubMed1976

lacY mutant of Escherichia coli with altered physiology of lactose induction.

A mutant of Escherichia coli is described that grew on lactose only in the presence of isopropylthiogalactoside. This cell contained a defect in the lacY gene that resulted in the formation of a transport system with a poor affinity for lactose. The inability to grow on lactose alone was due to the failure of induction by this disaccharide. This failure of inducation was presumably due to a defect in lactose accumulation which resulted in significant reduction in the formation of allo-lactose, the true inducer of lac operon. These results are consistent with the view that the capacity to accumulate lactose plays an important physiological role in the induction of the enzymes necessary for its utilization.

Biological Transport, Active↗
PubMed1976

Speculations on the evolution of ion transport mechanisms.

Primate cells evolved a plasma membrane to restrict the loss of important molecules. The osmotic problems that then arose were solved in one of several ways. Of major importance was the evolution of specific ion pumps, to actively extrude those salts whose inward diffusion would have led to swelling and lysis. In addition, these pumps allowed the cell to store energy in the form of ion gradients across the membrane. Thus, even in the earliest stages, the evolution of ion transport systems coincided with the development of mechanisms which catalyzes the energy transformations. It is postulated that an "ATP"-driven proton pump was one of the first ion transport systems. Such a proton pump would extrude hydrogen ions from the cell, establishing both a transmembrane pH gradient (alkaline inside) and a membrane potential (negative inside). This difference in electrochemical potential for protons (the proton-motive force) could then drive a variety of essential membrane functions, such as the active transport of ions and nutrients. A second major advance was the evolution of an ion transport system that converted light energy into a form which could be used by the cell. The modern model for this is the "purple membrane" of Halobacterium halobium, which catalyzes the extrusion of protons after the capture of light. The protonmotive force generated by such a light-driven proton pump could then power net synthesis of ATP by a reversal of the ATP-driven proton pump. A third important evolutionary step associated with ion transport was the development of a system to harness energy released by biological oxidations. Again, the solution of this problem was to conserve energy as a protonmotive force by coupling the activity of a respiratory chain to the extrusion of protons. Finally, with the development of animal cells a more careful regulation of internal and external pH was required. Thus, an ATP-driven Na+-K+ pump replaced the proton-translocating ATPase as the major ion pump found in plasma membranes.

Adenosine Triphosphatases↗
PubMed1975

D-Alanine-requiring cell wall mutant of Escherichia coli.

A mutant of Escherichia coli is described whose cells show a spherical or irregular morphology, associated with leakage of beta-galactosidase and other intracellular proteins. The expression of the morphologic abnormality is most marked when the mutant is grown in rich media and is suppressed by D-alamine, D-serine, D-glutamate, or glycine supplementation. D-Alanine is the most effective amino acid supplement, half maximally supressing this anomalous property at a concentration of 75 mug/ml, as measured by the reduction in beta-galactosidase released from the cells. The mutant is more sensitive to penicillin G, D-methionine, and D-valine and it is relatively resistant to lysozyme. These phenotypic abnormalities are likewise corrected by the above supplementations. The relative rates of peptidoglycan synthesis in mutant and parent, grown under restrictive conditions, were measured both in vivo and in vitro by rates of incorporation of L-[14-D]alanine and uridine-5'-diphosphate-N-acetyl-D-[1-15C-A1-glucosamine, respectively. There is not metabolic block in the biosynthesis of uridine-5'-diphosphate-N-acetyl-muramyl-pentapeptide as shown by enzymic analysis and the lack of accumulation of uridine-5'-diphosphate-N-acetylmuramyl-peptide precursors. These preliminary studies suggest that the mutant possesses a defect in the biosynthesis of peptidoglycan although the exact lesion has not yet been established.

Alanine↗
PubMed1974

A protonmotive force drives ATP synthesis in bacteria.

When cells of Streptococcus lactis or Escherichia coli were suspended in a potassium-free medium, a membrane potential (negative inside) could be artificially generated by the addition of the potassium ionophore, valinomycin. In response to this inward directed protonmotive force, ATP synthesis catalyzed by the membrane-bound ATPase (EC 3.6.1.3) was observed. The formation of ATP was not found in S. lactis that had been treated with the ATPase inhibitor, N,N'-dicyclohexylcarbodiimide, nor was it observed in a mutant of E. coli lacking the ATPase. Inhibition of ATP synthesis in S. lactis was also observed when the membrane potential was reduced by the presence of external potassium, or when cells were first incubated with the proton conductor, carbonylcyanidefluoromethoxyphenylhydrazone. These results are in agreement with predictions made by the chemiosmotic hypothesis of Mitchell.

Adenosine Triphosphatases↗
PubMed1973

Proton-coupled accumulation of galactoside in Streptococcus lactis 7962.

When cells of the anaerobe Streptococcus lactis 7962 are deprived of their normal fermentable energy source, active transport of galactosides is completely abolished although the membrane carriers are still capable of facilitating the equilibration of sugars across the cell membrane. In these nonmetabolizing cells it was possible to test the Mitchell hypothesis of obligatory coupling of proton movement with sugar transport. This hypothesis was supported by alkalinization of the medium observed when thiomethylgalactoside was added to a lightly buffered suspension of S. lactis cells. Conversely, addition of protons resulted in active transport of thiomethylgalactoside. Accumulation of thiomethylgalactoside to a concentration more than 20-times that in the external medium was induced by suddenly exposing cells to a medium at pH 6; no accumulation of thiomethylgalactoside was observed with cells exposed to pH 8.Active transport of thiomethylgalactoside occurred in the absence of energy metabolism when S. lactis cells were treated with valinomycin. This ionophore allowed intracellular K(+) to flow out, thus imposing a membrane potential (inside negative). This potential resulted in a proton uptake and an associated active transport of galactoside. The membrane potential was measured from the distribution ratio (inside/outside) of K(+) in the presence of valinomycin. The pH gradient was measured from the distribution ratio of [(14)C]methylamine. The protonmotive force, calculated from the membrane potential and the pH gradient, was found to be directly related to the accumulation of galactoside, in accordance with the chemiosmotic hypothesis.

Biological Transport, Active↗
PubMed1972

Role of metabolic energy in the transport of -galactosides by Streptococcus lactis.

Streptococcus lactis (ATCC 7962) accumulated thiomethyl-beta-galactoside (TMG) and other galactosides against concentration gradients when the cells were supplied with a metabolizable substrate, such as glucose. The accumulated TMG was free and not phosphorylated. In the absence of glucose, TMG rapidly entered the cell to a concentration equal to that of the medium. Agents that uncouple oxidative phosphorylation abolished active transport but not the carrier-facilitated entry of TMG. Evidence that the transport carriers were functional in the absence of glucose or in the presence of uncoupling agents included the demonstration of counterflow, which depends on competitive inhibition for the carrier for exit.

Arginine↗