This study assesses the effects of storage temperature on postmortem changes in textural parameters (firmness, water holding capacity), and their relationship with biochemical and electrophoretic determinations (muscle collagen content and solubility, amount and integrity of sarcoplasmic and myofibrillar proteins) in sea bream muscle. Storage at 1C resulted in a prolongation of the firmness compared with 4C, with no noticeable changes in water holding capacity. This delay in muscle softening at 1C could be partially explained by a limited proteolysis of some myofibrillar proteins, although inconsistent tendency was observed for other fractions. In contrast, the rate of muscle collagen degradation was higher at 4C compared with 1C, this becoming the main contributing factor to firmness losses. The great variety of protein fractions separated electrophoretically, and the relatively minor and contradictory changes observed suggest the unfeasibility of electrophoresis as a routine procedure for studying freshness in stored sea bream.