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In this study, effect of gender, muscle type (<em>biceps femoris</em> (BF) and <em>longissimus thoracis</em> (LT)) and storage time (14 days) on the proteolytic pattern of camel meat myofibrillar proteins was investigated using SDS-PAGE. Heavy chain myosin (MHC) and actin changed little during postmortem aging of muscles. Proteolysis intensity of MHC in female camels was significantly more than male ones (<em>P</em><0.05). Degradation of C-protein was influenced by storage time, gender and muscle type (<em>P</em><0.05). α-actinin was proteolyzed by catepsins at the second week of aging, and its breakdown was more pronounced in BF than LT muscle (<em>P</em><0.05). Principal degradation of desmin   occurred at the first week of storage. Troponin-T was proteolyzed by about 80% up to 5 days of storage, and muscle type and aging time significantly affected its proteolysis. The30 kDapolypeptideas a main product of Troponin-T degradation began to appear 24 h postmortem, and its band intensity increased significantly during 14 days of storage (<em>P</em><0.05). In conclusion, storage time was the most important factor affecting degradation of myofibrillar proteins during storage at 4^oC. Also, muscle type was a main factor at proteolysis of desmin cytoskeletal protein and some regulating proteins (α-actinin and Troponin-T).