GLUTAMINE METABOLISM IN EHRLICH ASCITES-CARCINOMA CELLS
GLUTAMINE METABOLISM IN EHRLICH ASCITES-CARCINOMA CELLS
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DOI：
10.1042/bj0830284
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发表时间：
1962-01-01
影响因子：
4.1
通讯作者：
JOHNSTONE, RM
中科院分区：
文献类型：
--
作者：
COLES, NW;JOHNSTONE, RM
埃利希腹水癌细胞中谷氨酰胺的氧化通过α-酮戊二酸和三羧酸循环的其他中间产物进行。在缺乏足够合适的乙酰辅酶A前体的细胞中，谷氨酰胺的氧化导致天冬氨酸的形成。在产生乙酰辅酶A的物质存在下，谷氨酰胺的氧化速率降低，但氧化程度增加。碳酸氢钠和α-含氧酸可增加谷氨酰胺氧化速率。在厌氧条件下，丙酮酸、草酰乙酸和苯丙酮酸可抑制氨基酸与蛋白质的结合。谷氨酰胺可特异性逆转这种抑制作用。在需氧条件下，苯丙酮酸可抑制氨基酸与蛋白质的结合，而谷氨酰胺、丙酮酸、草酰乙酸和葡萄糖可逆转这种抑制作用。谷氨酰胺在某些情况下可以作为能量来源，用于这些细胞将氨基酸掺入蛋白质中。
The oxidation of glutamine in Ehrlich ascites-carcinoma cells proceeds through a-oxoglutarate and other intermediates of the tricarboxylic acid cycle. In cells lacking sufficient suitable precursors of acetyl-coenzyme A, the oxidation of glutamine results in the formation of aspartic acid. In the presence of substances giving rise to acetyl-coenzyme A, the rate of oxidation of glutamine is decreased, but the extent of oxidation is increased. The rate of glutamine oxidation is increased by sodium hydrogen carbonate and a-oxo acids. The incorporation of amino acids into proteins is inhibited under anaerobic conditions by pyruvate, oxaloacetate and phenylpyruvate. This inhibition is reversed specifically by glutamine. The incorporation of amino acids into proteins is inhibited under aerobic conditions by phenylpyruvate, and this inhibition is reversed by glutamine, pyruvate, oxaloacetate and glucose. Glutamine may serve as a source of energy under certain circumstances for the incorporation of amino acids into proteins by these cells.