Degradation of Ubiquitin in Beef During Storage

摘要

Sarcoplasmic proteins were prepared from the quadriceps femoris muscle immediately after slaughter 92.5 hr) and from stored muscle samples at 10 days post mortem for SDS-PAGE analysis and Western blotting. Characterization with ubiquitin antiserum (Signma, St. Louis, MO, USA) showed clear and strong recognition of ubiquitin (8.6 kDa) and another minor Band (17 kDa) in purified ubiquitin (Sigma, St. Louis, MO, USA). Among the sarco- plasmic proteins prepared, this antiserum also reacted with the bands corresponding to purified ubiquitin (8.6 kDa and 17 kDa) and a small amount of some other higher-molecular- Mass proteins which were considered to be ubiquitin-protein conjugates.