| Summary: | RNAlater<sup>®</sup> is regarded as a potential preservation method for proteins, while its effect on bovine muscle proteins has rarely been evaluated. Bovine muscle protein samples (<i>n</i> = 12) collected from three tender (Warner⁻Bratzler shear force: 30.02⁻31.74 N) and three tough (Warner⁻Bratzler shear force: 54.12⁻66.25 N) Longissimus thoracis et lumborum (LTL) samples, preserved using two different sampling preservation methods (RNAlater<sup>®</sup> and dry ice), at two <i>post mortem</i> time points (day 0 and day 14), were characterized using one-dimensional electrophoresis. Fourteen bands with molecular weights ranging from 15 to 250 kDa were verified, both in the dry ice and RNAlater<sup>®</sup> storage groups, at each time point, using image analysis. A shift from high to low molecular weight fragments, between day 0 and day 14, indicated proteolysis of the muscle proteins during post mortem storage. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses and database searching resulted in the identification of 10 proteins in four bands. Protein profiles of muscle preserved in RNAlater<sup>®</sup> were similar to those of muscle frozen on dry ice storage, both at day 0 and day 14. The results demonstrate that RNAlater<sup>®</sup> could be a simple and efficient way to preserve bovine muscle proteins for bovine muscle proteomic studies.
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