摘要 : BACKGROUND: In this study the interspecies differences in two-dimensional electrophoresis patterns of skeletal muscle myosin light chain (MLC) isoforms between <i>Bos taurus</i> (cattle), <i>Sus scrofa</i> (pig), <i>Gallus gallus<... 展开 BACKGROUND: In this study the interspecies differences in two-dimensional electrophoresis patterns of skeletal muscle myosin light chain (MLC) isoforms between <i>Bos taurus</i> (cattle), <i>Sus scrofa</i> (pig), <i>Gallus gallus</i> (chicken), <i>Meleagris gallopavo</i> (turkey), <i>Anas platyrhynchos</i> (duck) and <i>Anser anser</i> (goose) were characterised on the basis of specific properties of MLCs associated with their structure and mobility in gel. RESULTS: Two-dimensional electrophoresis separations revealed species-specific differences in the molecular weight and pI of individual MLC isoforms (MLC1f, MLC2f and MLC3f). In the case of closely related animal species such as goose and duck or turkey and chicken, significant differences occurred in MLC1f. For MLC2f, differences between cattle and turkey and between pig and chicken were around 1 and 0.3 kDa respectively. It appeared from the comparison of amino acid sequences that even MLCs with only 2% difference in sequences have different electrophoretic mobilities. CONCLUSION: Interspecies differences in skeletal MLC isoforms appeared between cattle, pig, chicken, turkey, duck and goose. The slight changes observed in the course of the aging process confirmed that these proteins are relatively little susceptible to proteolytic enzymes during meat aging.Digital Object Identifier http://dx.doi.org/10.1002/jsfa.4486 收起