Cold-acclimatization and intermediary metabolism of carbohydrates

Morrison, George R.; Brock, Frances E.; Sobral, Dejano T.; Shank, Robert E.

doi:10.1016/0003-9861(66)90373-0

Cited by 31 publications

(5 citation statements)

References 29 publications

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“…All enzyme assays were demonstrated to be linear with time and with protein concentration. The marker enzymes assayed were: y-glutamyltranspeptidase (Tate & Meister, 1974), alkaline phosphatase (Scholer & Edelman, 1979), phosphoenolpyruvate carboxykinase (Seubert & Huth, 1965), ,J-glucuronidase ) (measured at 37°C); succinateand NADPH-cytochrome c reductase (Sottocassa et al, 1967), lactate dehydrogenase (Morrison et al, 1966) and hexokinase (Vinuela et al, 1963), measured at room temperature. We assayed four enzymes of arginine metabolism: argininosuccinate synthase, argininosuccinate lyase, arginase and orthinine aminotransferase.…”

Section: Enzyme Assaysmentioning

confidence: 99%

Cellular and subcellular localization of enzymes of arginine metabolism in rat kidney

Dhanakoti

Brosnan

Herzberg

et al. 1992

Biochemical Journal

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Rat kidneys extract citrulline derived from the intestinal metabolism of glutamine and convert it stoichiometrically into arginine. This pathway constitutes the major endogenous source of arginine. We investigated the localization of enzymes of arginine synthesis, argininosuccinate synthase and lyase, and of breakdown, arginase and ornithine aminotransferase, in five regions of rat kidney, in cortical tubule fractions and in subcellular fractions of cortex. Argininosuccinate synthase and lyase were found almost exclusively in cortex. Arginase and ornithine aminotransferase were found in inner cortex and outer medulla. Since cortical tissue primarily consists of proximal convoluted and straight tubules, distal tubules and glomeruli, we prepared cortical tubule fragments by collagenase digestion of cortices and fractionated them on a Percoll gradient. Argininosuccinate synthase and lyase were found to be markedly enriched in proximal convoluted tubules, whereas less than 10% of arginase and ornithine aminotransferase, were recovered in this fraction. Arginine production from citrulline was also enriched in proximal convoluted tubules. Subcellular fractionation of kidney cortex revealed that argininosuccinate synthase and lyase are cytosolic. We therefore conclude that arginine synthesis occurs in the cytoplasm of the cells of the proximal convoluted tubule.

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Section: Enzyme Assaysmentioning

confidence: 99%

Cellular and subcellular localization of enzymes of arginine metabolism in rat kidney

Dhanakoti

Brosnan

Herzberg

et al. 1992

Biochemical Journal

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“…Succinateand NADPH-cytochrome c reductase activities were assayed as described by Sottocasa et al (1967); f-glucuronidase as described by Gianetto and deDuve (1955); lactate dehydrogenase as described by Morrison et al (1966); orithine-2-oxo acid aminotransferase as described by Pegg et al (1970). Assay for ornithine decarboxylase Ornithine decarboxylase activity was measured by following the release of 14CO2 fromn L-[1-"4C]ornithine, by using a modification of the method of Pegg & Williams-Ashman (1968).…”

Section: Enzyme Assaysmentioning

confidence: 99%

Subcellular localization of ornithine decarboxylase in liver of control and growth-hormone-treated rats

Murphy¹,

Brosnan²

1976

Biochemical Journal

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1. Ornithine-2-oxo acid aminotransferase activity was inhibited by amino-oxyacetate (10(-5) M). This permitted the measurement of ornithine decarboxylase in the presence of mitochondria by using the 14CO2-trapping technique. 2. Subcellular fractionation of rat liver by differential centrifugation, followed by the assay of ornithine decarboxylase in the presence of amino oxyacetate and of marker enzymes for each fraction, demonstrated that ornithine decarboxylase was located in the cytosol. 3. The greatly increased ornithine decarboxylase activity observed after growth-hormone administration was also found to be localized in the cytosol. 4. The Km of ornithine decarboxylase from rat liver for ornithine was 28 muM. Administration of growth hormone 4 h before death did not affect the apparent affinity of ornithine decarboxylase for ornithine.

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“…Succinate-and NADPH-cytochrome c reductases were measured according to Sottocasa et al [7], /3-glucuronidase according to Gianetto and de Duve [8], lactate dehydrogenase according to Morrison et al [9]. Adenylate kinase was assayed by the method of Schnaitman and Greenawalt [6] except that 0.33 mM sodium sulfide replaced KCN as a cytochrome oxidase inhibitor.…”

Section: Enzyme Assaysmentioning

confidence: 99%