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Biomedical subjects

R F Palmer

Publications and source records attributed to R F Palmer.

At least 73 records · Page 4Linked to original sources

Drug interactions.

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Drug Synergism↗

Strontium-90: effects of chronic ingestion on farrowing performance of miniature swine.

In experiments involving the ingestion of strontium-90 by nearly 800 female miniature swine and extending over three generations, no significant differences in litter size, percentage of stillborn, or birth weight were observed between controls and animals ingesting up to 625 microcuries of strontium-90 per day. At 625 microcuries per day, these animals were ingesting more than a million times the peak value of strontium-90 ever reported in the American diet. Animals on 3100 microcuries per day did not survive the gestation period. From these studies, it is evident that feeding levels of strontium-90 high enough to affect fetal or neonatal mortality in this species will not permit maternal survival long enough for the bearing of young.

Animals↗

Calcium and adenosine triphosphate binding to renal membranes.

Calcium binds to membranous structures isolated from rabbit kidney cortex homogenates. The binding is enhanced by ATP and Mg(++) in combination. Other nucleotides, ITP and GTP, do not have this property. In contrast to similar preparations of nerve and muscle, the binding is not augmented by oxalate (3-100 mM). Also, binding of calcium cannot be correlated with ATP hydrolysis. p-Chloromercuribenzoate and the mercurial diuretic agent mercaptomerin inhibit the binding of calcium. This system can be distinguished from the binding of calcium by mitochondria by lack of azide inhibition and by failure of ADP-succinate to substitute for ATP. (14)C- and gamma-(32)P-labeled ATP bind to the renal membranes in the absence of calcium, but only the (32)P binding increases when calcium is added. The ratio of (32)P bound to (45)Ca bound is 2:1. The above data are consistent with a hypothesis that calcium is metabolically bound to renal membranes and that this binding is associated with membrane phosphorylation. Such a formulation may have pertinence to the conformational state of renal membranes and subsequent permeability characteristics. It also allows for the concept that membrane stability requires metabolic participation, as well as calcium ions.

Adenosine Triphosphatases↗