The superoxide dismutase activity of various photosynthetic organisms measured by a new and rapid assay technique

Henry, Landis E. A.; Halliwell, Barry; Hall, D.O.

doi:10.1016/0014-5793(76)80527-3

Cited by 41 publications

(7 citation statements)

References 23 publications

(25 reference statements)

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“…Activity was calculated according to Asada et al [20]. Column fractions in the course of enzyme purification were assayed as described by Henry et al [21]. Protein content of crude fractions and purified enzyme was determined according to Lowry et al [22] and Murphy and Kies I231 respectively using bovine serum albumin as a standard for both methods.…”

Section: Enzyme and Protein Assaysmentioning

confidence: 99%

“…Leaf extract was applied to a column following ammonium sulfate precipitation and DEAE-Sephadex A-SO batch steps. Superoxide dismutase activity is expressed as a percentage of inhibition, by a given aliquot of the eluate, of the reaction of nitroblue tetrazolium (NBT) reduction by K f O - [21] from subsequent centrifugation (12000 x g, 1 h) was dissolved and dialyzed for 40 h against 10 mM potassium phosphate, pH 7.8, containing 5 mM 2-mercaptoethanol and 0.1 mM EDTA. The dialysate was brought to 200 mM phosphate with 1 M potassium phosphate, pH 7.8, and DEAE-Sephadex A-50 (20 m1/100 ml solution), pre-equilibrated with 200 mM potassium phosphate containing 0.1 mM EDTA, was added.…”

Section: Purification Of the Enzymementioning

confidence: 99%

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Isolation and characterization of an iron‐containing superoxide dismutase from tomato leaves, Lycopersicon esculentum

Kwiatowski

Safianowska

Kaniuga

1985

European Journal of Biochemistry

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Section: Enzyme and Protein Assaysmentioning

confidence: 99%

Section: Purification Of the Enzymementioning

confidence: 99%

Isolation and characterization of an iron‐containing superoxide dismutase from tomato leaves, Lycopersicon esculentum

Kwiatowski

Safianowska

Kaniuga

1985

European Journal of Biochemistry

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“…One activity unit is defined as that amount of enzyme that inhibits by 50% the reduction of Nitro-Blue Tetrazolium under the conditions of Halliwell (1975). In addition, the potassium superoxide method was used to assay column eluates (Henry et al, 1976;except that the reaction was carried out in 0.1 M-potassium phosphate, pH7.8). The effect of cyanide on the superoxide dismutase activity was examined by the inclusion of 1 mM-KCN (pH 7.8) in the reaction mixture.…”

Section: Measurements Ofenzyme Activitiesmentioning

confidence: 99%

Intracellular localization, isolation and characterization of two distinct varieties of superoxide dismutase from Neurospora crassa

Henry

Cammack

Schwitzguébel

et al. 1980

Biochemical Journal

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1. Neurospora crassa was found to contain two distinct superoxide dismutases. 2. Most of the activity is associated with the cytosolic fraction and was shown to be the Cu/Zn-containing form of the protein. 3. Mitochondria isolated from Neurospora crassa showed two distinct superoxide dismutases: a cyanide-sensitive Cu/Zn-containing protein and a cyanide-insensitive form which probably contains manganese. 4. Localization experiments, using selective marker enzymes and digitonin fractionation, indicated that the cyanide-sensitive form is localized in the intermembrane space, whereas the cyanide-insensitive form is confined to the mitochondrial matrix space. 5. The cytosolic Cu/Zn-containing superoxide dismutase was isolated in high yields and extensively characterized by using e.p.r. spectroscopy, isoelectric focusing and analytical ultracentrifugation. 6. E.p.r. spectroscopy was used to monitor changes in the copper environment of the native protein after the addition of a number of potential inhibitors and after high-pH treatment. 7. Both of the cyanide-sensitive Cu/Zn-containing enzymes (cytosolic and mitochondrial) appeared to have identical properties which in turn were different from the cyanide-insensitive enzyme. 8. It is probable that the cyanide-insensitive enzyme was not previously detected, owing to its low amount (less than 10% of the total activity), greater lability than the cyanide-sensitive enzyme and the necessity of obtaining a mitochondrial-enriched fraction before its isolation.

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“…Superoxide dismutase was assayed by three different methods: the xanthine/xanthine oxidase system (Halliwell, 1975), the riboflavin/methionine system (Beauchamp & Fridovich, 1971) and the K02 method (Henry et al, 1976). Nitro Blue Tetrazolium was used in each of the assay systems and the development of the blue colour caused by formazan production was followed at 560nm.…”

Section: Enzyme Assaysmentioning

confidence: 99%

Superoxide dismutase and catalase in the protection of the proton-donating systems of nitrogen fixation in the blue-green alga Anabaena cylindrica

Henry¹,

Гоготов²,

Hall³

1978

Biochemical Journal

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1. Superoxide dismutasel activity was present in the heterocysts and vegetative cells of Anabaena cylindrica, but was always lower in the heterocysts. 2. No qualitative differences were found in the superoxide dismutase from the two cellular types. 3. Catalase activity was also present in both cellular types. 4. Most of the NADP reductase activity, as assayed with menadione or ferredoxin as electron acceptor, was localized within the heterocysts. 5. Studies on H2 consumption showed that most of the hydrogenase activity was associated with the heterocysts. 6. The results are discussed in terms of the postulate that superoxide dismutase and catalase are involved in the protection of the protondonating systems participating in N2 fixation and H2 metabolism of heterocysts.

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The superoxide dismutase activity of various photosynthetic organisms measured by a new and rapid assay technique

Cited by 41 publications

References 23 publications

Isolation and characterization of an iron‐containing superoxide dismutase from tomato leaves, Lycopersicon esculentum

Isolation and characterization of an iron‐containing superoxide dismutase from tomato leaves, Lycopersicon esculentum

Intracellular localization, isolation and characterization of two distinct varieties of superoxide dismutase from Neurospora crassa

Superoxide dismutase and catalase in the protection of the proton-donating systems of nitrogen fixation in the blue-green alga Anabaena cylindrica

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