Nuclear magnetic resonance study of muscle water protons in muscular dystrophy of chickens
- 1 April 1981
- journal article
- research article
- Published by Wiley in Journal of Cellular Physiology
- Vol. 107 (1) , 139-145
- https://doi.org/10.1002/jcp.1041070115
Abstract
Using the pulsed nuclear magnetic resonance (NMR) spectroscopy, the spin‐lattice (T1) and the spin‐spin (T2) relaxations times of water protons from samples of pectoralis major muscles of normal (line 412) and homozygous dystrophic (line 413) chickens were measured. Both the T1 and T2 were significantly increased (P < 0.05) in the dystrophic muscles. The mean values of the relaxation times are given ± S.D. The T1 values were 654 ± 22 msec in normal and 692 ± 41 msec in dystrophic muscles. The T2 values for normal and dystrophic muscles were 39 ± 4 msec and 52 ± 7 msec, respectively. Although the water content of dystrophic muscles (78.9 ± 0.6%) determined by gravimetric methods was significantly higher than normal muscles (74.9 ± 1.1%), this difference in tissue hydration could not explain quantitatively the increase of T1 and T2 values in the dystrophic muscles. The results of the measurements of the relaxation times seem to suggest that there are changes in the composition and/or conformational state of the proteins.This publication has 42 references indexed in Scilit:
- MYOSIN IN HEREDITARY MUSCULAR DYSTROPHY OF CHICKENS*Annals of the New York Academy of Sciences, 2006
- RELEVANCE OF GENETIC ANIMAL MODELS OF MUSCULAR DYSTROPHY TO HUMAN MUSCULAR DYSTROPHIES *Annals of the New York Academy of Sciences, 1979
- RELATIONSHIP BETWEEN MYOSIN STRUCTURE AND MUSCLE DEGENERATIONAnnals of the New York Academy of Sciences, 1979
- BIOCHEMICAL STUDIES OF DYSTROPHY IN THE YOUNG CHICKEN: LYSOSOMAL AND SARCOLEMMAL ENZYMESAnnals of the New York Academy of Sciences, 1979
- MAJOR PHYSIOLOGIC AND HISTOCHEMICAL CHARACTERISTICS OF INHERITED DYSTROPHY OF THE CHICKEN *Annals of the New York Academy of Sciences, 1979
- The measurement of cross-relaxation effects in the proton NMR spin-lattice relaxation of water in biological systems: Hydrated collagen and muscleJournal of Magnetic Resonance (1969), 1978
- Calcium transport and phosphoenzyme formation in sarcoplasmic reticulum isolated from normal and dystrophic chickensBiochemical Medicine, 1977
- Myofibrillar proteins of developing and dystrophic skeletal muscleFEBS Letters, 1976
- Ca2+ transport and assembly of protein particles in sarcoplasmic membranes isolated from normal and dystrophic muscleFEBS Letters, 1975
- Effects of Diffusion on Free Precession in Nuclear Magnetic Resonance ExperimentsPhysical Review B, 1954