Search PubMed⌕ Search

Biomedical subjects

R D Batt

Publications and source records attributed to R D Batt.

At least 19 recordsLinked to original sources
PubMed1985

Increased malate dehydrogenase activity in blood from non-drinking alcoholics.

Since cytosolic malate dehydrogenase has been shown to play a role in the regulation of liver cytosolic [NAD+]/[NADH] redox state during ethanol metabolism, it is possible that differences in this enzyme could cause differences in response to ethanol. The present study demonstrates that the isozyme pattern of this cytosolic enzyme in whole blood samples is the same as that in liver and that the pattern does not differ in alcoholic and control subjects. A marginally significant elevation of activity of malate dehydrogenase in blood from alcoholic subjects is reported. Further studies are needed to confirm this latter finding and to assess fully its possible significance.

Alcoholism↗
PubMed1979

Obesity indices.

Explore the source record for details and available documents.

Adipose Tissue↗
PubMed1976

Inhibition of RNA synthesis in Chlorella pyrenoidosa and Bacillus megaterium by the pine-blight toxin, dothistromin.

Dosthistromin, an anthraquinone derivative produced by the pine-blight fungus, Dothistroma pini, inhibits the growth of Chlorella pyrenoidosa and Bacillus megaterium. At growth inhibitory concentrations, dothistromin strongly inhibits incorporation of [3H]uridine into RNA of both species. With B. megaterium, marked inhibition of [3H]uridine incorporation is apparent within 5 min of addition of dothistromin, but only a slight inhibition of [3H]thymidine incorporation into the DNA-containing fraction or of [14C]leucine incorporation into protein is detectable after 10 min.

Anthraquinones↗
PubMed1972

Deficiency of alpha-mannosidase in Angus cattle. An inherited lysosomal storage disease.

A disease of Angus cattle previously known as pseudolipidosis has been shown to be an inherited lysosomal storage disease, in which an oligosaccharide containing mannose and glucosamine is the storage substance. Diseased animals have a near-absolute deficiency of the lysosomal enzyme, alpha-mannosidase, whereas heterozygotes have a partial deficiency of this enzyme. The condition is analogous to the human disease known as mannosidosis.

Animals↗