[124] “Malic”-enzyme

Ochoa, Severo

doi:10.1016/0076-6879(55)01129-4

Cited by 482 publications

(89 citation statements)

References 15 publications

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“…Fecal neutral and acidic steroids were measured by gas-liquid chromatography using an OV-17 (Chromatotec, Tokyo) column 32) and an AN-600 (Chromatotec) column 33) respectively. The activities of cytosolic fatty acid synthase (FAS), 34) glucose-6-phosphate dehydrogenase (G6PDH), 35) the malic enzyme, 36) microsomal phosphatidate phosphohydrolase (PAP), 37) and mitochondrial carnitine palmitoyltransferase (CPT) 38) were determined in the liver. Protein was assayed by the method of Lowry et al, 39) using bovine serum albumin as a standard.…”

Section: Methodsmentioning

confidence: 99%

Effects of Dietary Oyster Extract on Lipid Metabolism, Blood Pressure, and Blood Glucose in SD Rats, Hypertensive Rats, and Diabetic Rats

Tanaka

Nishizono

Kugino

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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Section: Methodsmentioning

confidence: 99%

Effects of Dietary Oyster Extract on Lipid Metabolism, Blood Pressure, and Blood Glucose in SD Rats, Hypertensive Rats, and Diabetic Rats

Tanaka

Nishizono

Kugino

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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“…The assay method for hepatic and renal phenylalanine hydroxylase activity was as described by Greengard & DelValle (1976). Previously established methods were used for the assay of tyrosine aminotransferase (EC 2.6.1.5) (Lin et al, 1958), soluble and mitochondrial aspartate aminotransferase (EC 2.6.1.1) (Herzfeld & Greengard, 1971) and the malate dehydrogenase (EC 1.1.1.37) (Ochoa, 1955) activities of liver extracts. The assay for glutaminase (EC 3.5.1.2) and succinate dehydrogenase (EC 1.3.99.1) activities in the particulate fraction of cerebral hemispheres (hereafter referred to as 'brain') were those of Huang (1974) and Laatsch et al (1962).…”

Section: Methodsmentioning

confidence: 99%

The regulation of phenylalanine hydroxylase in rat tissues in vivo. The maintenance of high plasma phenylalanine concentrations in suckling rats: a model for phenylketonuria

Delvalle

Greengard

1976

Biochemical Journal

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Maximum inhibition of phenylalanine hydroxylase activity in the liver (85 %) and in the kidney (50%) of suckling rats required the administration of over 9,pmol of p-chlorophenylalanine/lOg body weight. Despite the decrease in the total activity from 184 to 34 units per lOg body weight, the injection of as much as 26fmol of phenylalanine was required for its concentration in plasma to be still considerably elevated 12h later. In rats injected with p-chlorophenylalanine every 48h and with phenylalanine every 24h from 3 to 18 days of age, the hepatic and renal phenylalanine hydroxylase remained inhibited, whereas the activities of three other hepatic enzymes were unchanged. There was about 20 % inhibition of brain and body growth, but no interference with the developmental formation of several cerebral enzymes (four dehydrogenases, hexokinase and glutaminase) was detected. In the course of this prolonged treatment, the phenylalanine concentrations in plasma increased gradually; on day 2 and day 8 (measured 12h after the last injection) they were 800 and 1395 nmol/ml respectively; on day 15, 12 and 18h after the usual injection, the values were 2030 and 1030 respectively as opposed to the 96nmol in untreated rats. This degree of hyperphenylalaninaemia, persisting for 18h per day throughout a critical period of development, fulfils the primary criterion of a suitable animal model for phenylketonuria.

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“…Analysis of Fatty Acid Synthesizing Enzymes-Fatty acid synthetase (15), malic enzyme (ME) (16), ATP-citrate lyase (17), acetyl-CoA carboxylase (18), and glucose-6-phosphate dehydrogenase (19) were measured as described previously.…”

Section: Materials-sodiummentioning

confidence: 99%

Altered Constitutive Expression of Fatty Acid-metabolizing Enzymes in Mice Lacking the Peroxisome Proliferator-activated Receptor α (PPARα)

Aoyama¹,

Peters²,

Iritani³

et al. 1998

Journal of Biological Chemistry

811

597

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Peroxisome proliferator-activated receptor ␣ (PPAR␣) is a member of the steroid/nuclear receptor superfamily and mediates the biological and toxicological effects of peroxisome proliferators. To determine the physiological role of PPAR␣ in fatty acid metabolism, levels of peroxisomal and mitochondrial fatty acid metabolizing enzymes were determined in the PPAR␣ null mouse. Constitutive liver ␤-oxidation of the long chain fatty acid, palmitic acid, was lower in the PPAR␣ null mice as compared with wild type mice, indicating defective mitochondrial fatty acid catabolism. In contrast, constitutive oxidation of the very long chain fatty acid, lignoceric acid, was not different between wild type and PPAR␣ null mice, suggesting that constitutive expression of enzymes involved in peroxisomal ␤-oxidation is independent of PPAR␣. Indeed, the PPAR␣ null mice had normal levels of the peroxisomal acyl-CoA oxidase, bifunctional protein (hydratase ؉ 3-hydroxyacyl-CoA dehydrogenase), and thiolase but lower constitutive expression of the D-type bifunctional protein (hydratase ؉ 3-hydroxyacyl-CoA dehydrogenase). Several mitochondrial fatty acid metabolizing enzymes including very long chain acyl-CoA dehydrogenase, long chain acyl-CoA dehydrogenase, short chain-specific 3-ketoacyl-CoA thiolase, and long chain acylCoA synthetase are also expressed at lower levels in the untreated PPAR␣ null mice, whereas other fatty acid metabolizing enzymes were not different between the untreated null mice and wild type mice. A lower constitutive expression of mRNAs encoding these enzymes was also found, suggesting that the effect was due to altered gene expression. In wild type mice, both peroxisomal and mitochondrial enzymes were induced by the peroxisome proliferator Wy-14,643; induction was not observed in the PPAR␣ null animals. These data indicate that PPAR␣ modulates constitutive expression of genes encoding several mitochondrial fatty acid-catabolizing enzymes in addition to mediating inducible mitochondrial and peroxisomal fatty acid ␤-oxidation, thus establishing a role for the receptor in fatty acid homeostasis.

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[124] “Malic”-enzyme

Cited by 482 publications

References 15 publications

Effects of Dietary Oyster Extract on Lipid Metabolism, Blood Pressure, and Blood Glucose in SD Rats, Hypertensive Rats, and Diabetic Rats

Effects of Dietary Oyster Extract on Lipid Metabolism, Blood Pressure, and Blood Glucose in SD Rats, Hypertensive Rats, and Diabetic Rats

The regulation of phenylalanine hydroxylase in rat tissues in vivo. The maintenance of high plasma phenylalanine concentrations in suckling rats: a model for phenylketonuria

Altered Constitutive Expression of Fatty Acid-metabolizing Enzymes in Mice Lacking the Peroxisome Proliferator-activated Receptor α (PPARα)

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