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| Differential Proteomics Analysis of Fresh and Refrigerated longissimus dorsi Muscles of Organically Raised Yaks from the Qinghai-Tibetan Plateau |
| JIA Jianlei1, ZHANG Qinwen1, ZHANG Hongjian1, LI Li1, DING Xin1, LI Hongzheng2, ZHAO Jing1,* |
| 1. College of Agriculture and Animal Husbandry, Qinghai University, Xining 810016, China;2. Qinghai Lücaoyuan Food Co. Ltd., Xining 810000, China |
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Abstract This paper proposes a methodology for investigating the differential proteomics of fresh and refrigerated
longissimus dorsi muscles of organically raised yaks from the Qinghai-Tibetan plateau. Protein extraction from longissimus
dorsi muscles was performed through ultrasonic cell disruption. The extracted protein was quantitated by the Bradford
method and analyzed by two-dimensional electrophoresis (2-DE). PD Quest gel image analysis software was used to
screen ≥ 3-fold differential protein spots for analysis by matrix-assisted laser desorption/ionization time of flight/time-offlight
mass spectrometry (MALDI-TOF-TOF-MS) and the proteins were identified using Mascot software. The results
showed that 1 840±181 and 2 034±86 protein spots from fresh and refrigerated longissimus dorsi muscles, distributed in
the pH range of 3.0–10.0, were respectively observed in the 2-DE gels. A total of 36 protein spots with ≥ 3-fold differences
from fresh and refrigerated muscles were screened out, including 12 upregulated ones and 24 downregulated ones in fresh
longissimus dorsi as compared to refrigerated longissimus dorsi. Seven differential protein spots of significance (with a score
greater than 65) were identified by mass spectrometry (MS), 2 of which were up-expressed and 5 down-expressed.
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