Nature and Distribution of Glycolic Acid Oxidase in Plants.

Noll, Clifford R.; Burris, R. H.

doi:10.1104/pp.29.3.261

Cited by 25 publications

(3 citation statements)

References 11 publications

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“…The similarity of the rates in both light and dark indicate the complete suppression of photosynthesis. The results are in agreement with those of El-Sharkawyet al (6) Glycolic acid oxidase activity in wheat, corn and oats has been demonstrated by manv workers (18,21,22). Hess and Tolbert (12,23) failed to detect glvcolic acid oxidase activity in some unicelluilar algae and have generalized to state that "glycolate metabolism represents a major difference between algae and higher plants".…”

Section: Resultssupporting

confidence: 82%

Photorespiration and Glycolate Metabolism: A Re-examination and Correlation of Some Previous Studies

Downton

Tregunna

1968

Plant Physiol.

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A bstract. Some previous studies of photorespiration and glycolate oxidation were reexamined and correlated by infra-red CO, analysis. Data about rate of photosynthesis and oxygen sensitivity indicated that complete inhibition of photosynthesis with 3. (3,4-dichlorophenyl) -1,1 dimethyl urea (DCMU) allowed dark respiration to continue in the light. Photorespiration was also inhibited. The oxygen senisitivity of glycolate-stimulated CO2 production was found to be compatible with the proposal that glycolate is a substrate of photorespiration. B-oth 'in vivo' and 'in vitro' studies of the alga Nitella flexilis have revealed a pathway of glycolate oxidation similar to that of higher plants. DCMU inhibition of photosynthesis by Nitella gave results similar to those for the monocotyledons tested. Under very low light intensity, carbon dioxide compensation in corn was measurable but was not sensitive to high oxygen concentration. It appears that the lack of photorespiration in this plant is not the end result of efficient internal recycling of CO, to photosynthesis.Photorespiration has been described as a CO, producing process that operates during photosynthesis in some leaves and algae. The newer evidence supporting this concept is based on the response of photorespiration to 0. concentration. It has been shown that dark respiration in leaves is saturated by about 2 % 02 whereas photorespiration has a much higher 0., requirement (7,25). 'Much recent literature also implicates glycolic acid as a substrate of photorespiration. The correlation which we have studied is the O., requirement for glycolate-stimulated CO, production. These results led to another studv of whether corn leaves produce CO., by photorespiration during photosynthesis.A recent paper by El-Sharkawy et al. (6) has provided data on CO. production in the light and dark when C0, source-sink relationships were changed by inhibiting photosynthesis with DCM\IU.Under these conditions the rates in light and dark were identical and these data were used as evidence for a common source of CO, evolved both during photosynthesis and in the dark. We re-examined this work and extended it with information about the effect of 02 tension on rates of CO., production.As a check against the possibility that the gas exchange results from the DCMU-treated monocotyledons were an artifact of stomatal behavior, the gas exchange of a DCMU-treated alga, Nitella flexilis, was studied. This alga has been shown to have a photorespiratory mechanism similar to that of some land plants (3). Results obtained by inhibiting photosynthesis by non-chemical means have

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Section: Resultssupporting

confidence: 82%

Photorespiration and Glycolate Metabolism: A Re-examination and Correlation of Some Previous Studies

Downton

Tregunna

1968

Plant Physiol.

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“…A high CO2 compensation point in these plants reflects Consequently, it might be predicted that such plants would contain little or no glycolate oxidase. Although investigation failed to observe significant glycolate oxidase activity in corn (22), the enzyme has been reported in this plant by other workers (10,19,20). The metabolism of added glycolate-14C by corn leaves to glycine and serine also suggests the existence of an active glycolate pathway in this species (15,27).…”

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confidence: 87%

A Survey of Plants for Leaf Peroxisomes

et al. 1969

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Abstract. Leaves of 10 plant species, 7 with photorespiration (spinach, sunflower, tobacco, pea, wheat, bean, and Swiss chard) and 3 without photorespiration (corn, sugarcane, and pigweed), were surveyed for peroxisomes. The distribution pattern for glycolate oxidase, glyoxylate reductase, catalase, and part of the malate dehydrogenase indicated that these enzymes exist together in this organelle. The peroxisomes were isolated at the interface between layers of 1.8 to 2.3 M sucrose by isopycnic nonlinear sucrose density gradient centrifugation or in 1.95 M sucrose on a linear gradient. Chloroplasts, located by chlorophyll, and mitochondria by cytochrome c oxidase, were in 1.3 to 1.8 M sucrose.In leaf homogenates from the first 7 species with photorespiration, glycolate oxidase activity ran,ged from 0.5 to 1.5 ,rmoles X min-' X g71 wet weight or a specific activity of 0.02 to 0.05 Atmole X min-' X mgV protein. Glyoxylate reductase activity was oomparable with glycolate oxidase. Catalase activity in the homogenates ranged from 4000 to 12,000 /moles X min-' X g-' wet weight or 90 to 300 ,umoles X min'1 X mg7 protein. Specific activities of malate dehydrogenase and cytochrome oxidase are also reported. In contrast, homogenates of corn and sugarcane leaves, without photorespiration, had 2 to 5 t% as much glycolate oxidase, glyoxylate reductase, and catalase activity. These amounts of activity, though lower than in plants with photorespiration, are, nevertheless, substantial. Peroxisomes were detected in leaf homogenates of all plants tested; however, significant yields were obtained only from the first 5 species mentioned above. From spinach and sunflower leaves, a maximum of about 50 %o of the marker enzyme activities was found to be in these microbodies after homogenization. The specific activity for peroxisomal glycolate oxidase and glyoxylate reductase was about 1 gmole X min-1 X mg-' protein; for catalase, 8000 tmoles X min-' X mg-1 protein,and for malate dehydrogenase, 40 ,mol.es X min-' X mg-' protein. Only small to trace amounts of marker enzymes for leaf peroxisomes were recovered on the sucrose gradients from the last 5 species of plants. Bean leaves, with photorespiration, had large amounts of these enzymes (0.57 umole of glycolate oxidase X min-' X g-1 tissue) in the soluble fraction, but only traces of activity in the peroxisomal fraction. Low peroxisome recovery from certain plants was attributed to particle fragility or loss of protein as well as to small numbers of particles in such plants as corn and sugarcane.Homogenates of pigweed leaves (no photorespiration) contained from one-third to one-half the activity of the glycolate pathway enzymes as found in comparable preparations from spinach leaves which exhibit photorespiration. However, only traces of peroxisomal enzymes were separated by sucrose gradient centrifugation of particles from pigweed. Data from pigweed on the absence of photorespiration yet abundance of enzymes associated with glycolate metabolism is inconsistent with current hypotheses ...

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“…The present paper gives further information about the changes in diseased tissues. Glycolic acid oxidase is one of the most widely distributed enzymes in the plant kingdom (KoLESNiKOV et al 1956, NOLL andBURRIS 1954) and its role in terminal oxidations also has been demonstrated (ZELITCH 1953). It seemed, therefore, to be of interest to correlate its activity with the characteristic respiratory response in infected host tissues.…”

Section: Introductionmentioning

confidence: 99%

Decline of Glycolic Acid Oxidase Activity in Flax Leaves Infected with Melampsora lini (Pers.) Lév.

Kakkar

1966

J Phytopathol

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Nature and Distribution of Glycolic Acid Oxidase in Plants.

Cited by 25 publications

References 11 publications

Photorespiration and Glycolate Metabolism: A Re-examination and Correlation of Some Previous Studies

Photorespiration and Glycolate Metabolism: A Re-examination and Correlation of Some Previous Studies

A Survey of Plants for Leaf Peroxisomes

Decline of Glycolic Acid Oxidase Activity in Flax Leaves Infected with Melampsora lini (Pers.) Lév.

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