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- W2041098081 abstract "Glycine is decomposed in rat brain cortex to yield carbon dioxide. This process, in which C 14 O 2 is formed from glycine-1-C 14 , is markedly stimulated by the presence of 10 mM glucose, the rate of production of C 14 O 2 being increased at least threefold. The presence of succinate exercises a much smaller stimulation of C 14 O 2 formation. The addition of KCl (0.1 M) or of 2,4-dmitrophenol (0.025 mM), whilst stimulating the rate of oxygen uptake, does not increase the rate of C 14 O 2 formation from glycine-1-C 14 . The addition of K + tends to diminish the rate. The process of glycine-1-C 14 breakdown to C 14 O 2 is almost insensitive to chlorpromazine, under the given experimental conditions, until relatively high concentrations (e.g. 0.6 mM) are used. The presence of chlorpromazine, however, brings about an inhibition of the rate of glycine-1-C 14 incorporation into rat brain cortex proteins, an inhibition of 20% being recorded at a concentration of the drug (0.2 mM) that has little or no effect on the respiration of the brain or on the rate of breakdown of glycine-1-C 14 into C 14 O 2 . Glycine incorporation into brain cortex proteins is a process relatively sensitive to chlorpromazine, the magnitude of inhibition being of the same order as that brought about by amytal at similar concentrations. It is suggested that chlorpromazine brings about its effects by an uncoupling of phosphorylation from oxidation in brain cortex slices." @default.
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- W2041098081 date "1957-12-01" @default.
- W2041098081 modified "2023-09-27" @default.
- W2041098081 title "BIOCHEMICAL STUDIES ON CHLORPROMAZINE: 2. EFFECTS OF CHLORPROMAZINE ON INCORPORATION INTO PROTEINS, AND BREAKDOWN OF GLYCINE-1-C14BY ISOLATED RAT BRAIN CORTEX" @default.
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- W2041098081 doi "https://doi.org/10.1139/o57-131" @default.
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