Electrophoretic Behavior of Cross-linked Myosin Heavy Chian in Suwari Gel.

Abstract

The electrophoretic behavior of cross-linked myosin heavy chain (CMHC) in suwari gel from Alaska pollack frozen surimi was investigated. The suwari gel set at 30°C was solubilized in 8 Murea-2% SDS-2% 2-mercaptoethanol-20mM Tris-HCl buffer (pH 8.0) and subjected to SDS-poly-acrylamide gel electrophoresis (SDS-PAGE). As the setting was prolonged, the band due to myosin heavy chain (MHC) weakened with the strengthening of the band due to CMHC at the top of the disk gel. However, more MHC and less CMHC were found when SDS-PAGE was performed in the presence of 8M urea. The CMHC was extracted with the above buffer from the top 5mm portion of the disk gel after the SDS-PAGE, and electrophoresed again. The MHC band reappeared along with a new protein band at 66k. The results suggest that the CMHC treated in this study was formed partly by the aggregation of MHC through weak bonds such as hydrogen and hydrophobic bonds.