Serine-Ethanolamine-Phosphate, Taurine and Free Amino Acids of Muscle in Hereditary Muscular Dystrophy of the Chicken.

Peterson, D. W.; Lilyblade, A. L.; Lyon, John B.

doi:10.3181/00379727-113-28494

Cited by 25 publications

(8 citation statements)

References 3 publications

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“…In general, these data agree with the findings of Miller et al (1965) for light meat of broilers and those of Peterson et al (1963) for the meat of hens. In general, these data agree with the findings of Miller et al (1965) for light meat of broilers and those of Peterson et al (1963) for the meat of hens.…”

Section: Resultssupporting

confidence: 90%

Free Amino Acids in Broiler Chicken Meat in Relation to Initial pH

Niewiarowicz¹,

Pikul²,

Trojan³

et al. 1978

Poultry Science

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The content of 13 free amino acids in broiler breast meat was measured by an automatic amino acid analyzer. Overall, free amino acid content of low pH meat (5.5 to 5.7) was significantly lower than that of intermediate pH meat (5.9 to 6.2), which in turn was lower than that of high pH meat (6.4 to 6.6). Overall, free amino acid content was significantly lower in fresh meat than in meat stored for 6 days at 4 C. Of the amino acids studied, alanine, threonine, and glutamic acid were present in high levels and methionine, phenylalanine, isoleucine, and proline in low levels. In fresh carcasses, the content of free amino acids was similar in meat at intermediate and high pH, but was significantly lower in meat at low pH. In stored carcasses, the content of free amino acids was similar in meat at low and intermediate pH and was significantly higher in meat at high pH.We determined the absolute content of

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Section: Resultssupporting

confidence: 90%

Free Amino Acids in Broiler Chicken Meat in Relation to Initial pH

Niewiarowicz¹,

Pikul²,

Trojan³

et al. 1978

Poultry Science

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“…The data in this paper, taken together with the results of others (3,4,(8)(9)(10), offer supportive evidence for involvement of the intracellular redox status in the pathogenesis of avian muscular dystrophy.…”

Section: Methodssupporting

confidence: 85%

“…If dystrophic muscle were capable of an induced synthesis of enzymes in response to free radicals and peroxides, it seemed possible that dystrophic muscle might also accumulate smallmolecule antioxidants to facilitate removal of excess damaging free radicals. In fact, the levels of reduced and oxidized glutathione are elevated in muscles of dystrophic chickens and mice (9)(10)(11).…”

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confidence: 99%

Enhancement of free radical reduction by elevated concentrations of ascorbic acid in avian dystrophic muscle.

Perkins¹,

Beth²,

Wilkerson³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

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It has been postulated that the degenerative process in dystrophic muscle results from increased concentrations of free radicals, eroxides, or lipid hydroperoxides. Therefore, the reduction of the free radical tanol (2,2,6,6-tetramethyl-4-iperidinol-1-oxyl) by extracts of muscles of dystrophic and normal chickens was studied. Pectoral (white) and thigh (red) muscles were used. For initial rate measurements, the various muscle extracts were added to an equal volume of 0.2 mM tanol. Reaction mixtures were introduced into the EPR cavity in a standard aqueous flat cell. Rates were measured by continuously monitoring the decrease in signal amplitude of the center (MI = 0) solution tanol EPR resonance line (in-phase first harmonic absorption signal). With extracts from dystrophic white muscle, the reduction rate was 75% faster than normal, whereas in dystrophic red muscle extracts the rate was normal. This agreed with previous observations that white muscle is more severely affected than red in dystrophic chickens. The primary reductant was identified as reduced ascorbic acid, and the rate of reduction of tanol correlated directly with the concentrations of ascorbic acid in the various muscle extracts as shown by chemical analysis. The results suggest an involvement of the intracellular redox status in the pathogenesis of avian muscular dystrophy. Avian (chicken) muscular dystrophy has been considered as a model for human muscular dystrophy, in particular Duchenne dystrophy (1). Avian dystrophy is characterized: (i) by muscle weakness and atrophy, which is apparent when the bird is placed on its back and cannot right itself; (ii) by contractures or stiffness of the wings, which cannot be elevated beyond a horizontal plane; and (iii) biochemically, by increased levels of muscle enzymes in the serum, for example, creatine kinase and aldolase (1). The chicken is a good model because of the natural anatomical separation of the white, fast fibers (pectoral) and red, slow fibers (thigh and gastrocnemius). In avian and Duchenne dystrophy, the white muscle fibers are much more severely affected than the red (1, 2).It has been postulated that the degenerative process in dystrophic muscle may result from increased concentrations of deleterious agents such as free radicals, peroxides, and lipid hydroperoxides (3, 4). These agents promote lipid peroxidation,

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“…Carnosine and anserine levels are lower than in normal birds (3). Fifty-one compounds were studied for their ability to compete with the sulfhydryl group for cupric ions.…”

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confidence: 99%