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Biomedical subjects

N Gruener

Publications and source records attributed to N Gruener.

At least 55 records · Page 3Linked to original sources
PubMed1979

Mutagenicity and transformation by recycled water.

Increased use of contaminated water and long-range plans for the direct use of recycled water necessitate a careful assessment of the potential health effect on the population. Selected in vitro assays were used to evaluate the mutagenic and carcinogenic potential of a concentrated, recycled water sample. It was found that the concentrated water induced mutagenicity in hamster lung cells and cellular transformation in human embryonic lung fibroblasts. The use of in vitro analyses in conjunction with epidemiologic studies in determining the human risks of environmental carcinogens is discussed.

Animals↗
PubMed1966

Temperature-dependence of activation and inhibition of rat-brain adenosine triphosphatase activated by sodium and potassium ions.

1. The adenosine-triphosphatase activity of rat-brain microsomes was measured between 0 degrees and 37 degrees . The stimulatory effect of Na(+) plus K(+) on the Mg(2+)-dependent adenosine-triphosphatase activity decreased sharply with decreasing temperature and became negligible at 0 degrees . An Arrhenius plot drawn from the experimental data showed two discontinuities: one at about 6 degrees and the other at about 20 degrees . 2. The increment in activity induced by Na(+) plus K(+) was more sensitive to oligomycin at lower than at higher temperatures, but the opposite was observed for ouabain. The action of oligomycin showed a biphasic character, since below a certain concentration it caused slight activation of Na(+)-plus-K(+)-activated adenosine triphosphatase. 3. Where oligomycin increased the activity of the enzyme, it also enhanced the accumulation of an acid-precipitable phosphorylated compound formed through the transfer of the gamma-phosphate group of [(32)P]ATP to the enzyme system. Stimulatory concentrations of oligomycin did not interfere with K(+)-mediated dephosphorylation of the intermediate, though high concentrations of oligomycin counteracted the effect of K(+). 4. The temperature profile of K(+)-stimulated microsomal phosphatase qualitatively resembled that of microsomal adenosine triphosphatase.

Journal Article↗