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Biomedical subjects

S Silver

Publications and source records attributed to S Silver.

At least 181 records · Page 10Linked to original sources

Potassium uptake in synchronous and synchronized cultures of Escherichia coli.

Criteria are presented for distinguishing between synchronous and synchronized cultures (natural vs. forced synchrony) on the basis of characteristics of growth and division during a single generation. These criteria were applied in an examination of the uptake of potassium during the cell growth and division cycle in synchronous cultures and in a synchronized culture of Escherichia coli. In the synchronous cultures the uptake of (42)K doubled synchronously with cell number, corresponding to a constant rate of uptake per cell throughout the cell cycle. In the synchronized culture, uptake rates also remained constant during most of the cycle, but rates doubled abruptly well within the cycle. This constancy of (42)K uptake per cell supports an earlier interpretation for steady-state cultures that uptake is limited in each cell by a constant number of functional sites for binding, transport, or accumulation of compounds from the growth medium, and that the average number of such sites doubles late in each cell cycle. The abrupt doubling of the rate of uptake of potassium per cell in the synchronized culture appears because of partial uncoupling of cell division from activation or synthesis of these uptake sites.

Binding Sites↗

Valinomycin-induced uptake of potassium in membrane vesicles from Escherichia coli.

Osmotically shocked Escherichia coli and membrane vesicle ghosts from E. coli cells have lost the ability to accumulate potassium by active transport. The addition of valinomycin to the membrane ghosts restores the capacity to accumulate radioactive (42)K and (86)Rb by a temperature- and energy-dependent process. Membrane vesicles prepared from mutants of E. coli altered in potassium transport show defects in the valinomycin-stimulated accumulation of (42)K that are related to the defects in the intact cells.

Anti-Bacterial Agents↗

Colicin-tolerant mutants of Escherichia coli: resistance of membranes to colicin E1.

Colicin E1 blocks proline accumulation by membrane vesicles prepared from wild-type sensitive Escherichia coli. Two classes of mutant cells are unaffected by colicin. Vesicles from colicin-resistant strains are sensitive to colicin E1, whereas vesicles from colicin-tolerant strains are unaffected by colicin El. These results suggest that the colicin E1 receptor is on the cell membrane and that colicin-tolerant strains have altered membranes while colicin-resistant strains have altered cell walls.

Biological Transport↗

Manganese Active Transport in Escherichia coli.

Manganese was accumulated by cells of Escherichia coli by means of an active transport system quite independent of the magnesium transport system. When the radioisotope (54)Mn was used, manganese transport showed saturation kinetics with a K(m) of 2 x 10(-7)m and a V(max) of 1 to 4 nmoles/min per 10(12) cells at 25 C. The manganese transport system is highly specific; magnesium and calcium did not stimulate, inhibit, or compete with manganese for cellular uptake. Cobalt and iron specifically interfered with (54)Mn uptake, but only when added at concentrations 100 times higher than the K(m) for manganese. Active transport of manganese is temperature- and energy-dependent: uptake of (54)Mn was inhibited by cyanide, dinitrophenol, and m-chlorophenyl carbonylcyanide hydrazone (CCCP). Furthermore, the turnover or exit of manganese from intact cells was inhibited by energy poisons such as dinitrophenol and CCCP.

Journal Article↗

Active transport of magnesium in escherichia coli.

Magnesium-28 is accumulated by cells of Escherichia coli by a process that is temperature-dependent and inhibited by dinitrophenol and cyanide. The rate of uptake of magnesium is concentration-dependent, with a "K(m)" of about 5 x 10(-4)M in tryptone broth. There is evidence for cellular control over this rate. The magnesium accumulation system is specific, since neither potassium nor calcium (nor apparently manganese) competes with magnesium for cellular uptake. The magnesium that is accumulated by the cells can be released by treatment with toluene and partially exchanges with excess exogenous magnesium.

Biological Transport↗

Acridine binding by Escherichia coli: pH dependency and strain differences.

Acridine dye binding by cells of Escherichia coli has been characterized in terms of a number of parameters. There is a temperature-dependent, readily reversible binding of acriflavine which occurs to a greater extent with acridine-sensitive mutants of E. coli K-12 than with wild-type E. coli B or K-12. There is an essentially irreversible internal binding of acriflavine which occurs when the cellular permeability barriers are destroyed or altered by heat-treatment, elevated pH, treatment with toluene or phenethyl alcohol, or infection with bacteriophage T2 or T4. Both the reversible and the irreversible binding of acridines occurs more effectively with the acridine dye acriflavine than with the related dye proflavine, and still less effectively with 9-aminoacridine and quinacrine. These properties of acridine binding can be correlated with various inhibitory effects of the dyes on the cells.

Acridines↗

Action of steroidal diamines on active transport and permeability properties of Escherichia coli.

The steroidal diamine irehdiamine A (IDA) is a potent inhibitor of bacteriophage growth and macromolecular synthesis in Escherichia coli. By using radioactive (42)K and (14)C-thiomethylgalactoside (TMG), rapid effects of IDA and related steroids, both on the influx of potassium and TMG via their respective transport systems and on the efflux (leakage) of radioactivity from the treated cells, have been measured. IDA affects both the influx and efflux of (42)K at concentrations of steroid as low as 2 x 10(-5)m. Because of the increased leakage, it is not possible to tell whether there is a direct effect reducing the rate of active transport of potassium. The primary diamine, IDA, and its bis-secondary, bis-tertiary, and bis-quaternary diamine analogues are decreasingly effective in altering cell permeability properties in the order 1 degrees > 2 degrees > 3 degrees > 4 degrees . The effects of IDA on potassium transport are mirrored by similar effects on the transport of TMG. Therefore, the action of IDA is on the cell membrane and not directly on one or another transport system. The effects of IDA on cell permeability can reasonably explain the inhibitory actions of the drugs on bacteriophage growth and cellular metabolism.

Amines↗

Cation fluxes and permeability changes accompanying bacteriophage infection of Escherichia coli.

Infection of Escherichia coli by bacteriophage T2 was accompanied by a rapid but transient increase in the rate of loss of small molecules from the bacterial cells. This transient leakage was studied with radioactive labels such as (42)K and (28)Mg. Bacteriophage-induced leakage was dependent on the ratio of phage to bacteria: the higher the multiplicity of infection, the greater the leakage. No leakage occurred at 4 C [when adsorption proceeds but injection of phage deoxyribonucleic acid (DNA) is blocked]. Leakage was caused by heavily irradiated phage as well as by normal phage; therefore, the intracellular functioning of the bacteriophage DNA was not required. This conclusion was supported by experiments which showed phage-induced leakage in the presence of chloramphenicol or sodium cyanide. Leakage could be prevented by infecting the bacteria with phage in the presence of high magnesium concentrations. Phage-induced leakage was terminated by a "sealing" reaction, after which potassium turnover by infected and uninfected cells was very similar. The sealing reaction occurred even in the presence of chloramphenicol, suggesting that the sealing is controlled by bacterial and not bacteriophage genes. We were not able to detect any effect of normal bacteriophage infection on the influx (active transport) of potassium and magnesium into the cells.

Adsorption↗