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A R Foster

Publications and source records attributed to A R Foster.

6 recordsLinked to original sources
PubMed1994

Regulation of oxidative degradation of L-lysine in rat liver mitochondria.

The generation of 14CO2 from [1-14C]lysine by hepatic mitochondria through the saccharopine pathway is controlled by intramitochondrial concentrations of lysine, 2-oxoglutarate and NADPH. Mitochondria, isolated from rats pre-treated with glucagon, exhibited higher activities of L-lysine: 2-oxoglutarate reductase, saccharopine dehydrogenase and 2-aminoadipate aminotransferase. The flux through this pathway is stimulated in liver mitochondria after glucagon treatment. Multiple regulation of lysine oxidation in liver mitochondria confirms a complex mechanism of 'mitochondrial activation' by glucagon.

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PubMed1991

The effects of ovine growth hormone on protein turnover in rainbow trout.

Ovine growth hormone (oGH) was administered to rainbow trout via an intraperitoneal cholesterol implant. After 21 days, plasma oGH levels were recorded as control group, less than 2 ng ml-1, i.e., not detectable, and oGH group, 19.2 +/- 2.8 ng ml-1. oGH-treated fish exhibited significantly increased whole-body growth rates, whole-body protein accretion rates, stimulated tissue protein synthesis, and tissue protein accretion rates. A dramatic decrease in white muscle protein concentration was also observed after oGH treatment. In some tissues (liver and stomach), elevated protein synthesis rates were the result of higher RNA/protein ratios. However, in other tissues (gill and ventricle), increased RNA activity accounted for the differences in rates of protein synthesis. The growth promoting effects of oGH on both whole-body and tissue protein turnover were generally accompanied with no change in the efficiency of deposition of newly synthesized protein. For the same ration size, the oGH group showed higher retentions of ingested nitrogen. It is concluded that oGH significantly enhances whole-body growth rates as a result of the stimulatory effect on protein synthesis rates with little effect on protein degradation.

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