Purine nucleotide cycle enzymes in dystrophic and normal mouse muscle

1982 ◽  
Vol 2 (3) ◽  
pp. 177-183
Author(s):  
Peter S. Fitt ◽  
Matthew B. Parliament
Keyword(s):  
Comparative Study ◽  
Normal Mouse ◽  
Purine Nucleotide ◽  
Mouse Muscle ◽  
Dystrophic Mouse ◽  
Direct Assay ◽  
Purine Nucleotide Cycle

A comparative study of the operation of the purine nucleotide cycle and of the activity of adenylosuccinase in extracts of muscle from the two strains of dystrophic mouse shows that the cycle is defective in both cases in the conversion of adenylosuccinate to AMP. However, adenylosuccinase activity is only slightly reduced in the standard conditions for its direct assay.

scholarly journals Comparison of the protein-synthesizing machinery in the skeletal muscle of normal and dystrophic Bar Harbor mice

1969 ◽  
Vol 115 (3) ◽  
pp. 377-382 ◽  
Author(s):  
D. C. Watts ◽  
J. D. Reid
Keyword(s):  
Normal Mouse ◽  
Gradient Centrifugation ◽  
Absolute Difference ◽  
Similar Data ◽  
Dystrophic Muscle ◽  
Mouse Muscle ◽  
Dystrophic Mouse ◽  
Dna And Rna ◽  
Leg Muscle ◽  
Standard Protein

1. Although the total weight of leg muscle increased with the age of a normal mouse the DNA and RNA content per leg did not change significantly. 2. The weight of leg muscle from a dystrophic mouse was only about 45% of that from a normal mouse but the DNA and RNA contents were the same and hence similar DNA/RNA ratios were obtained. 3. The total ribosome contents of normal and dystrophic mice were the same on a whole-leg basis, and for both the free ribosomes were about 60% of the total. However, comparison with similar data from liver suggested that some loss of ribosomes occurred during the isolation procedure. 4. The polyribosome patterns obtained by density-gradient centrifugation were the same for normal and dystrophic muscle, and comparable polyribosome fractions of different sizes obtained from such gradients had similar capacities for the incorporation of radioactive amino acids in a standard protein-synthesizing system. 5. By using a standard protein-synthesizing system with normal polyribosomes similar extents of incorporation were found with normal- or dystrophic-muscle pH5 fraction or partially purified transfer RNA preparation. 6. It is concluded that there is no absolute difference between the protein-synthesizing systems of normal and dystrophic mouse muscle and that the observed apparent differences result from concentration differences caused by changes in muscle volume. 7. A possible cause of the failure of dystrophic muscle to resynthesize myofibrils is also suggested.

Enzyme studies of skeletal muscle in mice with hereditary muscular dystrophy

1963 ◽  
Vol 205 (5) ◽  
pp. 897-901 ◽  
Author(s):  
Marilyn W. McCaman
Keyword(s):  
Skeletal Muscle ◽  
Muscular Dystrophy ◽  
Glutathione Reductase ◽  
Enzyme Activities ◽  
Lactic Dehydrogenase ◽  
Normal Muscle ◽  
Dystrophic Muscle ◽  
Nerve Section ◽  
Mouse Muscle ◽  
Dystrophic Mouse

The activities of 20 enzymes in normal, heterozygous, and dystrophic mouse muscle were studied by means of quantitative microchemical methods. Enzyme activities in normal and heterozygous muscle were essentially the same. In dystrophic muscle glucose-6-P dehydrogenase, 6-P-gluconic dehydrogenase, glutathione reductase, peptidase, ß-glucuronidase, and glucokinase activities were significantly higher than in normal muscle, while α-glycero-P dehydrogenase and lactic dehydrogenase activities were significantly lower. The pattern of enzyme activities found in normal gastrocnemius denervated by nerve section was strikingly similar to that in dystrophic muscle.

scholarly journals The Purine Nucleotide Cycle

1972 ◽  
Vol 247 (1) ◽  
pp. 162-169 ◽  
Author(s):  
Keith Tornheim ◽  
John M. Lowenstein
Keyword(s):  
Purine Nucleotide ◽  
Purine Nucleotide Cycle

scholarly journals The role of glutamine oxidation and the purine nucleotide cycle for adaptation of tumour energetics to the transition from the anaerobic to the aerobic state

1988 ◽  
Vol 252 (2) ◽  
pp. 381-386 ◽  
Author(s):  
Z Kovacević ◽  
D Jerance ◽  
O Brkljac
Keyword(s):  
Adenine Nucleotide ◽  
The Other ◽  
Purine Nucleotide ◽  
Purine Nucleotide Cycle ◽  
Adenine Nucleotide Pool

It is proposed that the purine nucleotide cycle and glutamine oxidation play a key role in the adaptation of tumour energetics to the transition from the anaerobic to the aerobic state. In support of this proposal, it was found that glutamine and inosine markedly increase total adenylates in the presence of oxygen, whereas the addition of hadacidin abolishes this effect. Transition of the cells from the anaerobic to the aerobic state, and vice versa, in the presence of glutamine plus inosine revealed that there are two components of the adenine nucleotide pool, one which is stable and the other which is variable and responds to the aerobic-anaerobic transition. This part of the pool undergoes degradation or resynthesis owing to activation of the enzymes of the purine nucleotide cycle. Resynthesis of the pool is accompanied by substantial net utilization of aspartate, which is produced by glutamine oxidation. This is supported by the experiments in which the cells were alternately incubated with nitrogen or oxygen, demonstrating that hadacidin significantly decreased utilization of aspartate and regeneration of ATP owing to inhibition of adenylosuccinate synthase.

Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle

Nature ◽  
1977 ◽  
Vol 270 (5639) ◽  
pp. 725-727 ◽  
Author(s):  
DAVID YAFFE ◽  
ORA SAXEL
Keyword(s):  
Myogenic Cells ◽  
Mouse Muscle ◽  
Dystrophic Mouse

Binding of adenylosuccinate synthetase to contractile proteins of muscle

1989 ◽  
Vol 257 (1) ◽  
pp. C29-C35 ◽  
Author(s):  
J. P. Manfredi ◽  
R. Marquetant ◽  
A. D. Magid ◽  
E. W. Holmes
Keyword(s):  
Ionic Strength ◽  
Dissociation Constant ◽  
Thin Filament ◽  
Contractile Proteins ◽  
Purine Nucleotide ◽  
Apparent Dissociation Constant ◽  
Thin Filaments ◽  
Adenylosuccinate Synthetase ◽  
Purine Nucleotide Cycle ◽  
Low Ionic Strength

The muscle isozyme of adenylosuccinate synthetase (AdSS), an enzyme of the purine nucleotide cycle, has previously been shown to bind to purified F-actin in buffers of low ionic strength and pH (Ogawa et al. Eur. J. Biochem. 85: 331-338, 1978). We have extended these observations by measuring the association of both crude and purified AdSS with the contractile proteins of muscle in buffers of physiological ionic strength and pH. Under these conditions, the enzyme binds to F-actin, actin-tropomyosin complexes, reconstructed thin filaments, and myofibrils but not to myosin. The apparent dissociation constant of 1.2 microM and binding maximum of 2.6 nmol enzyme/mg myofibrils indicate that binding of AdSS to myofibrils can be physiologically significant. The results suggest that AdSS in muscle may be associated with the thin filament of myofibrils.

Muscle Purine Nucleotide Cycle Enzymes in Exercise Intolerance

1998 ◽  
pp. 205-209 ◽  
Author(s):  
Maria-Grazia Operti ◽  
M.-Françoise Vincent ◽  
Jean-Marie Brucher ◽  
Georges Van den Berghe
Keyword(s):  
Exercise Intolerance ◽  
Purine Nucleotide ◽  
Purine Nucleotide Cycle
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