The present paper reported postmortem changes in muscle proteins on sea bream (Sparus aurata), during ice storage. The postmortem evolution of protein patterns in farmed sea bream was monitored by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and two-dimension electrophoresis (2DE). Matrix associated laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) was used for identification of proteins. Results of the bio-informatics analysis demonstrate that: (1) the normalized volume of skeletal alpha-actin and tropomyosin is not affected by the time of storage; (2) the normalized volumes of myosin light chain 3 and of major histocompatibility complex (MHC) class II beta1 increase; (3) the normalized volumes of Sec 13-like and parvalbumin significantly decrease.
Identification by proteome analysis of muscle proteins in sea bream ( Sparus aurata )
SCHIAVONE, Roberta;ZILLI, Loredana;STORELLI, Carlo;VILELLA, Sebastiano
2008-01-01
Abstract
The present paper reported postmortem changes in muscle proteins on sea bream (Sparus aurata), during ice storage. The postmortem evolution of protein patterns in farmed sea bream was monitored by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and two-dimension electrophoresis (2DE). Matrix associated laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) was used for identification of proteins. Results of the bio-informatics analysis demonstrate that: (1) the normalized volume of skeletal alpha-actin and tropomyosin is not affected by the time of storage; (2) the normalized volumes of myosin light chain 3 and of major histocompatibility complex (MHC) class II beta1 increase; (3) the normalized volumes of Sec 13-like and parvalbumin significantly decrease.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
