Chicken Muscular Tissue

Nuclear Magnetic Resonance Studies of Interfacial Phenomena 

Characteristics of Water Bound in HGA Being in Different Media 

FIGURE 7.77 The muscle split into components and the locations of muscle water compartments the intra-myofibrillar component and the extra-myofibrillar component which is composed of the inter-myofibrillar, inter-fascicular, and extra-fascicular water populations. (According to Baechle, T.R. and Earle, R.W., Essentials of Strength Training and Conditioning, Second edition, Human Kinetics, Champaign, IL, 2008.) 

FIGURE 7.78 H NMR spectra of water bound in chicken muscular tissue at different hydrations Ch,o = (a) 0.4 and (b) 0.105 g/g. 

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Niacin determinations have similarly been performed by Lieck (1954) on samples of liver tissue, heart, and skclct il muscle obtained from calves and from adult cattle the analyses showed essentially ctiual niacin concentrations for the immature and the mature animals. In contrast to this, analyses made by Denton et al. (1947) on liver and muscular tissue specimens from chickens between 6 and 18 weeks of age revealed a definite decrease in the niacin levels of these tissues with age. 

To explain the CPK isoenzyme pattern in hereditary muscular dystrophy Schapira et al. (1968) and Cao et al. (1971) suggested that the organism simply fails to convert the fetal to the adult CPK pattern. Hooton and Watts (1966), however, claimed that hereditarily dystrophic mice contained an MM-CPK composed of two nonidentical subunits M and M. Fingerprints of the M polypeptide chain appeared to differ from those of the M subunit by a single peptide. Since the MM dimer showed only half the activity of the normal enzyme it was assumed that the M subunit was inactive. This would also explain why no M M enzyme was detected. Studies of CPK in dystrophic chickens and dystrophic humans could not confirm the existence of a distinct isoenzyme in dystrophic tissues (Roy et al, 1970). Should it exist, moreover, the question would remain whether this alteration is a specific feature of muscular dystrophy or whether it is the mere consequence of increased proteolysis in damaged muscle. 

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