Search PubMed⌕ Search

Biomedical subjects

R E Moore

Publications and source records attributed to R E Moore.

At least 145 records · Page 8Linked to original sources
PubMed1978

Latency of thyroid hormone action on heat production in the rat.

Euthyroid rats had an immediate calorigenic response to L 3-5-3' triiodothyronine (T3) 5 microgram/kg of about +10% lasting 8 hr and a somewhat greater response to T.S.H. Larger doses (50 microgram/kg) of T3 had a latency of 4-5 hr but the response was greater and lasted longer.

Animals↗
PubMed1977

Antileukemia activity in the Osillatoriaceae: isolation of Debromoaplysiatoxin from Lyngbya.

Chloroform extracts of several seaweeds, of the family Oscillatoriaceae, from Enewetak Atoll, Marshall Islands, display activity against P-388 lymphocytic mouse leukemia. A P-388 active compound, debromoaplysiatoxin, has been isolated from Lyngbya gracilis and characterized. This compound also has dermonecrotic activity and may be the dermatitis-producing substance in L. majuscula, the causative agent of "swimmers' itch" outbreaks in Hawaiian waters.

Animals↗
PubMed1976

Nalpha-acetylfusarinines: isolation, characterization, and properties.

The isolation, purification, and structural elucidation of a new group of naturally occurring hydroxamic acids are described. These compounds are produced by an unidentified species of Penicillium when grown on iron deficient medium. They are closely related structurally to the fusarinines, whose basic structure contains Ndelta-(cis-5-hydroxy-3-methylpent-2-enoyl)-Ndelta-hydroxy-L-ornithine, but the alpha-amino groups in the new compounds are protected by Nalpha acetyl groups. The most complex of the compounds is N,N',N"-triacetylfusarinine C, or N,N'N"-triacetylfusigen, a cyclic triester composed of three molecules on Nalpha-acetylfusarinine. The trimer has growth factor activity for Arthrobacter JG-9 about equal to fusarinine C itself. The monohydroxamate, Nalpha-acetylfusarinine, is more active than the trimer. The greater chemical stability of these compounds compared to the unacetylated fusarinines reconciles the utilization of otherwise unstable amino acid esters as iron transport agents.

Drug Stability↗
PubMed1976

Aspartate aminotransferase activity in human serum. Factors to be considered in supplementation with pyridoxal 5'-phosphate in vitro.

The pyridoxal phosphate reactivation of the apo form of aspartate aminotransferase (EC 2.6.1.1) in human serum has been studied with "normal" and above-normal activity of this enzyme. The extent of the reactionation did not depend on the presence of the substrates, L-aspartate or 2-oxoglutarate. Reactivation was greatest with 110 mumol of added pyridoxal phsophate present per liter during a preinucation for 7 min in tris(hydroxymethyl)methylamine buffer wit;h serum volume fractions ranging from 0.017 to 0.267. In comparison with measurements prformed with no exogenous pyridoxal phosphate present, we found two potential sources of error when this cofactor was added: (a) reagent and sample blanks in the pyridoxal phosphate-supplemented system were two- to eightfold higher and (b) progress curves were nonlinear when L-aspartate rather than 2-oxoglutarate was used as the startin substrate. Aspartate aminotransferase measurement sith pyridoxal phosphate supplementation was slightly more precise than without.

Acute Disease↗