Effect of proteasome inhibitor on sarcoplasmic protein of bovine skeletal muscle during storage
作者： M. Sekikawa , M. Yamamoto , M. Fukushima , K. Shimada , T. Ishikawa
DOI: 10.1016/S0308-8146(00)00272-7
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摘要: Bovine skeletal muscle, immediately after slaughter (1.5 h; 0 d), was buffered, homogenized treated with proteasome inhibitor, and stored (2 d) for SDS-PAGE Western blotting analysis. Ubiquitin antiserum (Sigma, St Louis) reacted bands corresponding to purified ubiquitin small amounts of other higher-molecular-mass proteins (about 30 40 kDa) which were considered be ubiquitin-protein conjugates. These faint in the control 2 d sample, suggesting that they had degraded. However, these tendencies positive decrease not clearly observed sample inhibitors (MG132 Lactacystin). results suggest both conjugates present muscle then degraded during storage. This degradation partially due action proteasome.
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