Sarcoplasmic protein profiles

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. 

Live and deproteinated plasma membranes of Acholeplasma laUawii were investigated by FTIR (Casal et al., 1980 Cameron et al., 1985). The temperature profiles of the gel to liquid crystalline phase transition of intact and deproteinated membranes, monitored by z/as(CD2), differ considerably. In intact membranes, the transition is broad and at temperatures within the range of the phase transition the live mycoplasma is able to keep the fluidity of its plasma membranes at a much higher level than that of the isolated plasma membrane. Native and reconstituted sarcoplasmic recticulum were investigated by Mendelsohn et al. (Mendelsohn et al., 1984). It appears that the protein Ca -ATPase interacts preferentially with the DOPC component of the membrane. A survey of these studies is available (Mantsch and McElhaney, 1991). 

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