Pyruvate

Bücher, Theodor; Czok, R.; Lamprecht, Walther; Latzko, Erwin

doi:10.1016/b978-0-12-395630-9.50055-4

Cited by 99 publications

(48 citation statements)

References 5 publications

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“…When 1,2,3-benzenetricarboxylate (50 mM) was added to the reaction medium, corresponding amounts of Tris-HCl were omitted. The incubation was terminated by addition of cold perchloric acid and after its precipitation by KHCO3, phosphoenolpyruvate was determined in the supernatant according to Bticher et al [8]. Protein was determined according to Lowry et al [9].…”

Section: Methodsmentioning

confidence: 99%

Phosphoenolpyruvate shuttle ‐ transport of energy from mitochondria to cytosol

et al. 1983

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Brown‐adipose tissue mitochondria of hamster and rat contain phosphoenolpyruvate carboxykinase (EC 4.1.1.32). In the presence of ketoglutarate and malate, phosphoenolpyruvate is formed and exported forms mitochondria. Phosphoenolpyruvate formation is inhibited by 1,2,3‐benzenetricarboxylate. It is proposed that phosphoenolpyruvate carboxykinase together with pyruvate carboxylase and pyruvate kinase forms a phosphoenolpyruvate shuttle through which energy produced by the Krebs cycle in mitochondria may be exported to cytosol.

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Section: Methodsmentioning

confidence: 99%

Phosphoenolpyruvate shuttle ‐ transport of energy from mitochondria to cytosol

et al. 1983

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“…D-Lactate was assayed according to Gawehn and Bergmeyer (1974); L-Iactate according to Gutman and Wahlefeld (1974); and pyruvate according to Bucher et al (1963). Protein was measured by the Biuret method using bovine plasma albumin as the standard (Gornall et al 1949).…”

Section: Assay Proceduresmentioning

confidence: 99%

Metabolism of D- and L-Lactate by Pseudomonas putida

Rw¹

1977

Aust. Jnl. Of Bio. Sci.

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Pseudomonas putida grew at the same rate with the same molar growth yield on D-, L, or DL-Iactate as the sole source of carbon for growth. D-and L-lactate were utilized simultaneously and at the same rate when the organism was grown on DL-Iactate (ratio of D isomer to L isomer of 1: 1). Growth on either isomer alone, or in combination, caused the induction of both a D-lactate, and an L-Iactate dehydrogenase. Both enzymes were particulate and used dichlorophenolindophenol, or oxygen, but not NAD, as electron acceptor, and were inhibited by cyanide when oxygen was the electron acceptor. The pH optimum for the D-lactate dehydrogenase was about 6·5, and for the L-Iactate dehydrogenase was about 8· O. The D-lactate dehydrogenase was more heat-sensitive than the L-Iactate dehydrogenase. The stoichiometry of both enzyme reactions was the same with 2 mol of lactate being oxidized by 1 mol of oxygen to form 2 mol of pyruvate. No lactate racemase was detected in the cell extracts. IntroductionThe metabolism of DL-Iactate by Pseudomonas aeruginosa (Kemp 1972) and P. citronellolis (O'Brien 1977) appears to depend on the induction ofNAD-independent D-and L-Iactate dehydrogenases. Growth of P. citronellolis on L-Iactate also induced both enzymes, but growth on D-Iactate induced only the D-Iactate dehydrogenase (O'Brien 1977). Pinchinoty et al. (1968) reported briefly that a soil organism, identified as P. putida, when grown on DL-Iactate, was capable of oxidizing D-or L-Iactate using oxygen or dichlorophenolindophenol (DCPIP) as electron acceptor. This paper presents evidence for the inducible nature of the D-and L-Iactate dehydrogenases of P. putida, and shows that the induction pattern differs from that of P. citronellolis. Some of the properties of the two lactate dehydrogenases are also described.

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“…Lactate and pyruvate were measured in freezeclamped biopsies [28,29]. Acid-soluble components were extracted from lyophilized tissue according to previously described methods [23].…”

Section: Determination Of the Hepatic Redox Statementioning

confidence: 99%

Control of Hepatic Protein Synthesis

Ayuso-Parrilla

Parrilla

1975

European Journal of Biochemistry

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The effect of nucleotide energy levels in vivo on the different steps of protein synthesis has been studied. Hepatic anoxia was induced by interrupting the blood portal-vein flow. At 5 min of anoxia ATP fell to 59 % of the control values and the amino acid incorporation into protein was inhibited by more than 70%. This strong inhibition was not paralleled by polyribosomal breakdown. On the contrary, when fasted rats were used, at 5 min of anoxia the ribosomal state of aggregation was found to increase. Longer periods of anoxia resulted in a further decrease in triphosphonucleoside content and polyribosomal breakdown. Based on these results and other reports from the literature it is concluded that the K, for the GTP of the peptide-chain-elongation mechanism must be higher than the K,,, of the initiation step. This finding implies that variations of nucleotide levels in vivo within the physiological range may control protein synthesis at the elongation step without apparent changes in the polyribosomal profiles.Most of the cellular functions are somehow related to the energy level of the cell, since the phosphorylation state of the adenine nucleotides is known to play a central role in metabolic regulation [l-31. On this subject there are in the literature several reports pointing to a clear relationship between energy level of the cell and rates of protein synthesis. It was found how anoxia inhibited the incorporation of amino acids into the proteins of several isolated rat tissues [4-61, of several tissues of the intact animals [7] and of isolated cell suspensions [8]. Not only anoxia but also the perturbation of the energetic level of the cell by other means results in an altered rate of protein synthesis [9, lo]. Nevertheless, it is not clear yet which of the steps involved in polypeptide synthesis, initiation, elongation or both, are under this type of control [ll -141. The problem has been approached in this work by studying the ribosomal state of aggregation as reflected by the polyribosomal profiles. The rationale of this approach lies in the fact that under normal conditions initiation and elongation are both synchronized in such a way that any perturbation on only one of them should bring about variations in the ribosomal pattern of aggregation. For instance, it is knowrn that the use of inhibitors of peptide chain

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Pyruvate

Cited by 99 publications

References 5 publications

Phosphoenolpyruvate shuttle ‐ transport of energy from mitochondria to cytosol

Phosphoenolpyruvate shuttle ‐ transport of energy from mitochondria to cytosol

Metabolism of D- and L-Lactate by Pseudomonas putida

Control of Hepatic Protein Synthesis

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