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Biomedical subjects

B A Davis

Publications and source records attributed to B A Davis.

152 records · Page 9Linked to original sources
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The effects of benzoate and fluoride on dental caries in intact and desalivated rats.

The decline in prevalence of dental caries in some segments of the population has been attributed mainly to extensive exposure to fluoride. Over the past decades, the use of fluoridated products has increased. During the same period, the consumption of food preservatives such as benzoates and sorbates has also increased substantially. Benzoates, in vitro, possess antibacterial properties similar to those of fluoride and in combination with fluoride could affect caries development. In the present study we explored the effects of sodium benzoate and fluoride in combination and alone on dental caries in our animal model. The results showed a combination of benzoate and fluoride reduced caries activity more effectively in rodents fed a cariogenic diet ad libitum than fluoride alone (p = 0.038).

Animals↗
PubMedDate not supplied

Mechanism of the stimulation of cardiac sarcoplasmic reticulum calcium pump by calmodulin.

Calmodulin has been shown to stimulate the initial rates of Ca2+-uptake and Ca2+-ATPase in cardiac sarcoplasmic reticulum, when it is present in the reaction assay media for these activities. To determine whether the stimulatory effect of calmodulin is mediated directly through its interaction with the Ca2+-ATPase, or indirectly through phosphorylation of phospholamban by an endogenous protein kinase, two approaches were taken in the present study. In the first approach, the effects of calmodulin were studied on a Ca2+-ATPase preparation, isolated from cardiac sarcoplasmic reticulum, which was essentially free of phospholamban. The enzyme was preincubated with various concentrations of calmodulin at 0 degrees C and 37 degrees C, but there was no effect on the Ca2+-ATPase activity assayed over a wide range of [Ca2+] (0.1-10 microM). In the second approach, cardiac sarcoplasmic reticulum vesicles were prephosphorylated by an endogenous protein kinase in the presence of calmodulin. Phosphorylation occurred predominantly on phospholamban, an oligomeric proteolipid. The sarcoplasmic reticulum vesicles were washed prior to assaying for Ca2+ uptake and Ca2+-ATPase activity in order to remove the added calmodulin. Phosphorylation of phospholamban enhanced the initial rates of Ca2+-uptake and Ca2+-ATPase, and this stimulation was associated with an increase in the affinity of the Ca2+-pump for calcium. The EC50 values for calcium activation of Ca2+-uptake and Ca2+-ATPase were 0.96 +/- 0.03 microM and 0.96 +/- 0.1 microM calcium by control vesicles, respectively. Phosphorylation decreased these values to 0.64 +/- 0.12 microM calcium for Ca2+-uptake and 0.62 +/- 0.11 microM calcium for Ca2+-ATPase. The stimulatory effect was associated with increases in the apparent initial rates of formation and decomposition of the phosphorylated intermediate of the Ca2+-ATPase. These findings suggest that calmodulin regulates cardiac sarcoplasmic reticulum function by protein kinase-mediated phosphorylation of phospholamban.

Animals↗
PubMedDate not supplied

Enzymatic N-methylation of phenelzine catalyzed by methyltransferases from adrenal and other tissues.

Phenelzine (2-phenylethylhydrazine) was found to be methylated by enzymes obtained from bovine adrenal and some rat tissues in the presence of S-adenosylmethionine as methyl group donor. The methylated product was chromatographically (TLC and HPLC) identical with chemically synthesized N-methylphenelzine and the structure of this methylated phenelzine has been confirmed by a GC/MS procedure. Methylation occurs at the terminal nitrogen of phenelzine. The phenelzine methyltransferase in the bovine adrenal has a molecular weight and isoelectric point identical with that of bovine adrenal phenylethanolamine N-methyltransferase. The affinity of phenelzine for the methyltransferase is quite high, i.e. KM = 6.5 x 10(-5) M. Methylated phenelzine possesses much weaker inhibitory activity toward monoamine oxidase (MAO). It can, however, be deaminated by MAO to produce phenylacetaldehyde, and subsequently phenylacetic acid. We have also observed that other hydrazine compounds, such as hydralazine, can be methylated by the adrenal enzyme. Our finding of enzymatic methylation of hydrazine compounds is novel and it may play a role in the metabolism of hydrazine drugs.

Adrenal Glands↗