Occurrence of Glycolate Dehydrogenase in Mitochondria and Microsomes in Streptomycin-Bleached Mutant of<i>Euglena gracilis</i>z

Yokota, Akiho; Kitaoka, Shôzaburô

doi:10.1080/00021369.1979.10863542

Cited by 5 publications

(5 citation statements)

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“…1979b), and then submitted to linear sucrose-density-gradient centrifugation (Yokota et al, 1978;). Succinic semialdehyde dehydrogenase as a marker for mitochondria (Tokunaga et al, 1976b(Tokunaga et al, , 1979 and NADPH-cytochrome c reductase as a marker for microsomal fraction (Omura & Takesue, 1970), mitochondria (Yokota & Kitaoka, 1979b) and chloroplasts (Lazzarini & Pietro, 1962) were assayed by the reported methods. Chlorophyll and protein 0306-3283/80/010377-04 $1.50/1 were determined respectively by the methods of MacKinney (1941) and Lowry et al (1951) (with bovine serum albumin as a standard).…”

Section: Methodsmentioning

confidence: 99%

Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase

Shigeoka¹,

Nakano²,

Kitaoka³

1980

Biochemical Journal

136

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Euglena gracilis was found to contain a peroxidase that specifically require L-ascorbic acid as the natural electron donor in the cytosol. The presence of an oxidation-reduction system metabolizing L-ascorbic acid was demonstrated in Euglena cells. Oxidation of L-ascorbic acid by the peroxidase, and the absence of ascorbic acid oxidase activity, suggests that the system functions to remove H2O2 in E. gracilis, which lacks catalase.

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Section: Methodsmentioning

confidence: 99%

Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase

Shigeoka¹,

Nakano²,

Kitaoka³

1980

Biochemical Journal

136

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“…The mutant contains no ribulose diphosphate carboxylase/oxygenase 28 ) and therefore glycolate can not be originated from ribulose diphosphate. IIi the mutant, glycolate might be derived from aromatic amino acids like in rat3 6 ) and/or from dihydroxyethylthiamine pyrophosphate like in Chromatium. 37 ) This problem awaits elucidation.…”

Section: Metabolism Of Glycolate In Intact Mitochondriamentioning

confidence: 99%

“…This was carried out in a manner described in the previous paper. 6 ) Action spectrum. Action spectrum of the photoinduction of glycolate dehydrogenase by monochromatic lights with a half-band width of IOnm was obtained according to the method of Shigeoka et al ll ) The light source was a short-arc Xenon lamp (6.5 kW) which was devised by KonishiY) The light intensity was determined with a thermopile and was 2,000 erg/cm 2 /sec over the region studied at the surface of cell suspension.…”

Section: Organism and Culturesmentioning

confidence: 99%

Occurrence and Subcellular Distribution of Enzymes Involved in the Glycolate Pathway and Their Physiological Function in a Bleached Mutant ofEuglena gracilisz

Yokota

Kitaoka

1981

Agricultural and Biological Chemistry

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“…3) ized in mitochondria in the bleached cells like A chloroplast-less mutant of Euglena is in the wild cells under non-photorespiratory readily prepared by the action of such mu-conditions, tagens as streptomycin, ultraviolet ray and high temperature. 4) Chloroplast DNAand MATERIALSANDMETHODS photosynthetic apparatus are depleted in such a mutant.5) In a preceding paper, 6) we have Organism and cultures. A chloroplast-less, bleached mutant of E. gracilis z was prepared by using streptof Metabolism ofGlycolateinEuglenagracilis.…”

mentioning

confidence: 99%

Metabolism of glycolate in Euglena gracilis. Part V. Occurrence and subcellular distribution of enzymes involved in the glycolate pathway and their physiological function in a bleached mutant of Euglena gracilis Z.

Yokota

Kitaoka

1981

Agricultural and Biological Chemistry

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The streptomycin-bleached, non-photosynthetic mutant of Euglena gracilis contained NADHglyoxylate reductase, NADPH-glyoxylate reductase, glutamate-glyoxylate aminotransferase and serine-glyoxylate aminotransferase, in addition to glycolate dehydrogenase. Most activities of NADH-and NADPH-glyoxylate reductases and 75% of glutamate-glyoxylate aminotransferase activity in the crude homogenate were recovered in mitochondria.The mutant cells grown under illumination contained three times as high glycolate dehydrogenase activity as the dark-grown cells. Illumination on the dark-grown cells caused an increase in activity to the level of the light-grown cells. Light at 420nm wavelength was most effective for inducing the enzyme. The enzyme induced by illumination was the mitochondrial one and the specific activity increased 4-fold after illumination for 3 days; the rate of the increase was almost equal to the ratio of the rate ofglycolate uptake from incubation mediumby the light-grown mutant to that of the dark-grown cells. However, there was no marked difference in the fate of carboxyl carbon of glycolate metabolized between the two types of cells.It is concluded from these results that mitochondrial glycolate dehydrogenase participates mainly in the glycolate metabolism in the bleached mutant. This is supported by experiments on the metabolism of glycolate in isolated, intact mitochondria of the mutant. The physiological significance of the formation and metabolism of glycolate in the non-photosynthetic mutant of Euglena was discussed.We have previously reported that in Euglena demonstrated that glycolate dehydrogenase is gracilis glycolate dehydrogenase, the key en-present in both mitochondria and microsomes, zyme of the glycolate pathway,1} is located in but not in microbodies, in the streptomycinboth mitochondria and microbodies.2) While bleached mutant of E. gracilis. Difference in the microbody enzymeis induced under the the subcellular distribution of this enzyme conditions favorable for the so-called photo-between the nonphotosynthetic mutant and respiration and it is presumably related to the the wild strain prompted us to study the photorespiratory metabolism of glycolate,2) metabolism and physiological function of the mitochondrial enzyme is not affected by glycolate in the mutant in comparison with these conditions and contributes to supplying that in the photosynthetic strain. The present glycine and serine for the synthesis of cellular paper makes it clear that glycolate is metabolproteins.3) ized in mitochondria in the bleached cells like A chloroplast-less mutant of Euglena is in the wild cells under non-photorespiratory readily prepared by the action of such mu-conditions, tagens as streptomycin, ultraviolet ray and high temperature.4) Chloroplast DNAand MATERIALSANDMETHODS photosynthetic apparatus are depleted in such a mutant.5) In a preceding paper,6) we have Organism and cultures. A chloroplast-less, bleached mutant of E. gracilis z was prepared by using streptof Metabolism ofGlycolateinEuglenagra...

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Occurrence of Glycolate Dehydrogenase in Mitochondria and Microsomes in Streptomycin-Bleached Mutant ofEuglena gracilisz

Cited by 5 publications

References 3 publications

Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase

Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase

Occurrence and Subcellular Distribution of Enzymes Involved in the Glycolate Pathway and Their Physiological Function in a Bleached Mutant ofEuglena gracilisz

Metabolism of glycolate in Euglena gracilis. Part V. Occurrence and subcellular distribution of enzymes involved in the glycolate pathway and their physiological function in a bleached mutant of Euglena gracilis Z.

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