‘Fatty acid peroxide’ formation in tissue homogenates from mice with hereditary myopathy (dystrophia muscularis)

Baker, Nome; Bloom, Alan S.; Blahd, William H.

doi:10.1152/ajplegacy.1959.197.2.483

Cited by 6 publications

(1 citation statement)

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“…the 'peroxide' amount on incubation was very much decreased. This effect has been observed with normal mouse-liver homogenate and occasionally also with brain (Baker, Bloom & Blahd, 1959), and has been attributed to inhibition of 'peroxide' formation, though it might equally reflect 'peroxide' destruction by ascorbic acid.…”

Section: Formation Of Thiobarbituric Acid Reactantsmentioning

confidence: 82%

Biochemical changes in the tissues of animals injected with iron. 3. Lipid peroxidation

Golberg¹,

Martin²,

Batchelor³

1962

Biochemical Journal

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Vol. 83 GLUTAMINE METABOLISM IN CARCINOMA CELLS 291oxidation of glutamine results in the formation of aspartic acid. 2. In the presence of substances giving rise to acetyl-coenzyme A, the rate of oxidation of glutamine is decreased, but the extent of oxidation is increased.3. The rate of glutamine oxidation is increased by sodium hydrogen carbonate and a-oxo acids.4. The incorporation of amino acids into proteins is inhibited under anaerobic conditions by pyruvate, oxaloacetate and phenylpyruvate. This inhibition is reversed specifically by glutamine.45. The incorporation of amino acids into proteins is inhibited under aerobic conditions by phenylpyruvate, and this inhibition is reversed by glutamine, pyruvate, oxaloacetate and glucose.6. Glutamine may serve as a source of energy under certain circumstances for the incorporation of amino acids into proteins by these cells.

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Section: Formation Of Thiobarbituric Acid Reactantsmentioning

confidence: 82%

Biochemical changes in the tissues of animals injected with iron. 3. Lipid peroxidation

Golberg¹,

Martin²,

Batchelor³

1962

Biochemical Journal

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Lipid peroxide and antioxidant enzymes in muscle and nonmuscle of dystrophic mouse

et al. 1989

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To determine whether abnormality in redox metabolism occurs specifically in certain individual dystrophic muscles, thiobarbituric acid reactivity, free radical scavengers, and oxidative marker enzymes were measured in the liver, kidney, erythrocytes, heart, and four different individual skeletal muscles from C57BL/6J dy/dy mice. Superoxide dismutases were assayed by specific radioimmunoassays, which enabled the study of a small individual murine muscle. Glutathione peroxidase and catalase were increased markedly in each individual dystrophic skeletal muscle studied and less markedly in the heart. Manganosuperoxide dismutase and thiobarbituric acid reactivity were decreased to a similar extent in each dystrophic skeletal muscle. Cuprozinc superoxide dismutase was decreased in the soleus muscle. Only a minimal biochemical change occurred in nonmuscles. Fumarase activity correlated closely with the level of manganosuperoxide dismutase. These results suggest that muscle protein breakdown occurs independently of lipid peroxidation despite the presence of tissue-specific abnormality of redox metabolism in dystrophic muscle.

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Die Biochemie der progressiven Muskeldystrophie

Heyck

Laudahn

1969

Die Progressiv-Dystrophischen Myopathien

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‘Fatty acid peroxide’ formation in tissue homogenates from mice with hereditary myopathy (dystrophia muscularis)

Cited by 6 publications

References 0 publications

Biochemical changes in the tissues of animals injected with iron. 3. Lipid peroxidation

Biochemical changes in the tissues of animals injected with iron. 3. Lipid peroxidation

Lipid peroxide and antioxidant enzymes in muscle and nonmuscle of dystrophic mouse

Die Biochemie der progressiven Muskeldystrophie

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