Muscle proteins, analysis

G7. Giometti, C. S., Anderson, N. G., and Anderson, N. L., Muscle protein analysis. 1. High-resolution two-dimensional electrophoresis of skeletal muscle proteins for analysis of small biopsy samples. Clin. Chem. 25, 1877-1884 (1979). 

Most of the studies indicate that denaturation of muscle proteins plays the dominant role in the quality changes of the frozen stored meats. The muscle proteins of fish and other aquatic animals have been found to be much less stable than those of beef animals, pigs and poultry (1 ). The present paper will be limited primarily to fish muscle as one representative of vertebrate muscle and it will also deal primarily with the behavior of fish proteins at sub-zero temperatures. In order to do a thorough analysis within the space limit permitted, focus will be on the changes of the proteins per se leaving peripheral problems to other reviews (2-18). 

It is probable that Bailey s first interest in the muscle field, in which lies his greatest contribution, was aroused by the work of Astbury and Dickinson who showed that fibers of denatured myosin behaved in ways similar to keratin so far as their elastic properties were concerned and their structures were revealed by X-ray analysis. At this time the Chibnall group was much interested in the amino acid composition of proteins. The obvious similarities in fibrous behavior between keratin and myosin despite their differences in amino acid composition, particularly in cystine content, stimulated Bailey to make a comparative study of the composition of some of the then recognized muscle proteins. This was Bailey s first paper on muscle and extension of the... 

Schmidt-Base, K. Buchbinder, J.L. Reed, G.H. Rayment, I. Crystallization and preliminary analysis of enzyme-substrate complexes of pyruvate kinase from rabbit muscle. Proteins Struct. Funct. Genet., 11, 153-157... 

An important potential application of the QLLS method to characterization of protein solutions stems from the fact, discussed above, that is quite small for solutions of rigid spheres. In systems of this type which exhibit substantial self-association, the major contribution to the apparent concentration dependence of Dt, derives from the association process which contributes a large negative term to the second virial coeflBcient. Herbert and Carlson (89) have reported a study of this type on the dimerization of the muscle protein myosin which indicates a value K = 1.30 dL/g for the association constant at lower concentrations of phosphate or sulfate (0.2M) and K = 10.6 dL/g at high concentrations (0.5M) (89). Chu et al. (90) have discussed some of the instrumental limitations of such analysis. 

Kjnrsgard JVH, Nprrelykke MR, Jessen F (2006). Changes in cod muscle proteins during frozen storage hy proteome analysis and multivariate data analysis. Proteomics, 6 1606-1618. 

CE has also been successfully apphed to the study of muscle proteins, and some of these applications have been recently reviewed. - - Methods for the determination of muscle proteins were based on CZE, SDS-CE, or isoelectric focusing (CEIF). Meat species identification was carried out by analyzing sarcoplasmic or myofibrillar proteins by a replaceable polymer-filled SDS-CE method (Table 30.8). However, the analysis of sarcoplasmic protein profiles allowed better differentiation among beef, pork, and turkey meat (Figure 30.8). The importance of sample preparation in the established method was highlighted since sarcoplasmic proteins extracted by simply homogenizing meat with cold bidistilled water were most useful for meat species identification when protein profiles were examined by linear discriminant analysis. On the other hand, myofibrillar proteins extracted with 0.6 M NaCl/0.01 M phosphate buffer with 0.5% polyphosphates (pH 6.0) were not useful for raw meat species identification, although they may be of importance in the identification of heat-processed meats. ... 

Muscle proteins are an important component of meat and can be classified according to solubility as sarcoplasmic (water soluble), myofibrillar (salt soluble), or stromal (insoluble) proteins. The application of CE to the analysis of meat proteins has been predominantly for separation of sarcoplasmic proteins in aqueous extracts from fish, bovine, and chicken muscle. The sarcoplasmic proteins that are present are mainly metabolic enzymes and therefore their separation profiles are useful for the purpose of species identification. Some reports also exist of the simultaneous separation of sarcoplasmic and myofibrillar meat proteins using SDS-CGE. 

When rainbow trout have been denied food for 6 days, meals bring about a post-prandial surge in protein synthesis in all the tissues (McMillan and Houlihan 1988). The time course of the protein synthesis response appears to be tissue-specific. Tissue protein synthesis rates in the ventricle and red and white muscle exhibited a graded response where a single meal resulted in synthesis rates lying between the fasted and continually fed states. The gill, stomach and intestine responded with a rapid rise within 3 h to the levels found in continually fed fish and this stimulation was maintained. The liver demonstrated a transient increase in protein synthesis which reached a peak at 3 h, which subsequently declined. Subsequent analysis has revealed that the peak found in the liver occurred within 1 h of the meal (McMillan and Houlihan 1989). A stimulation of muscle protein synthesis has been found in salmon 9 h after feeding (Fauconneau et al. 1989). 

Each disc was implanted subcutaneously in the back of a rat such that the protein film was in direct contact with the muscle tissue. The specimens remained in the animals for 1 week, 4 w eeks, and 7 weeks post implantation. At each time interval 6 specimens per polyoner group were retrieved for protein analysis. Additional specimens from each group were evaluated for tissue reaction by histolog). ... 

Serum analysis for diagnostic purposes is routinely carried out by paper electrophoresis. Other protems that have been satisfactorily analysed using paper electrophoresis include muscle protein, egg white proteins, milk proteins and snake and insect venoms etc. 

Gregory and Feldstein (94) developed an ion-paired, reversed-phase HPLC method for individual Be vitamers extracted with sulphosalicylic acid from different foods. Using a ternary solvent program, elution of nutritionally active Be vitamers from the analytical column was complete within 30 min. PLP was determined as its hydroxysulfonate derivative, following postcolumn introduction of a buffered solution of sodium bisulfite. This method was found suitable for vitamin Be analysis in foods of both plant and animal origin. Recoveries for PLP and PL from pork loin were <90% it was suggested that these vitamers were not completely released from muscle proteins, even in the presence of 5% sulfo-salicylic acid. 

Balti, R., Nedjar-Arroume, N., Yaba Adje, E., Guillochon, D., and Nasri, M. (2010) Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish Sepia officinalis) muscle proteins./. Agric. Food Chem., 58, 3840-3846. 

Electrophysiological studies often demonstrate multiple, asymmetric mononeuropathies, usually axonal in type, that cannot be localized to typical sites of entrapment (Keswani et al. 2002). CSF analysis reveals nonspecific abnormalities, such as elevated protein and mild mononuclear pleocytosis. Polymerase chain reaction (PCR) for CMV DNA and nerve or muscle biopsy may provide more specific diagnostic data (Roullet et al. 1994). 

Bradley WG, Shapshak P, Delgado S, Nagano I, Stewart R, Rocha B (1998) Morphometric analysis of the peripheral neuropathy of AIDS. Muscle Nerve 21 1188-1195 Brenneman DE, Westbrook GL, Fitzgerald SP, Ennist DL, Elkins KL, Ruff MR, Pert CB (1988) Neuronal cell killing by the envelope protein of HIV and its prevention by vasoactive intestinal peptide. Nature 335 639-642... 

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