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R D Batt

Publications and source records attributed to R D Batt.

9 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.

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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↗
PubMedDate not supplied

Effects of ethanol treatment and castration on liver alcohol dehydrogenase activity.

Induction of alcohol dehydrogenase (ADH) activity by chronic ethanol treatment and castration has previously been reported to occur in Sprague-Dawley rats. In the present study, no induction was found following chronic ethanol treatment and only a low level of induction was found with castration. However the activity of ADH was high in control animals compared with those used in other studies. The activity of ADH in control animals was not decreased by testosterone administration, which has been shown to reverse induction of the enzyme produced by chronic ethanol treatment or castration in other studies. It is concluded that the male Sprague-Dawley rat is not necessarily a suitable animal for the study of ADH induction by chronic ethanol treatment and that further unknown factors must be identified before the regulation of ADH activity in vivo is fully understood.

Alcohol Dehydrogenase↗