Different heat treatments, (1) chilled, 4°C (2) boiled at 100°C for 30 min and (3) autoclaved at 121°C at 15 psi for 20 min were employed on goat meat to mimic domestic and industrial cooking. The effects on intensity of actin proteins was observed using two-dimensional gel electrophoresis where significant differences (p>0.05) were observed in the spot intensity between chilled and boiled samples, similarly in chilled and autoclaved samples. However, no significant difference was observed between boiled and autoclaved samples. The slight changes observed in the cooking of meat confirmed that actin protein is susceptible to denaturation cause by heat. MALDI-TOF/TOF analysis revealed the peptide-mass fingerprint between positions 21 – 374 that not affected by heat treatment. Peptides from this position merit the candidature of actin as putative thermostable marker for detecting goat meat (chevon) in food product.
Gamma-tocotrienol (GTT) has been shown to exhibit significant antitumor activity in a variety of tumor cells. Previous findings have demonstrated that GTT had antiprolifera-tive effects on a liver cancer cell line (HepG2) with an IC50 value of 170μM. In this study, two dimensional gel electrophoresis (2DE) was used to determine changes in protein expression in HepG2 cell line following treatment with GTT. The ultimate aim is to identify the possible molecular mechanisms involved in GTT antitumor activity. This study is focused on obtaining a 2DE protein profile for HepG2 cell line with and without
GTT treatment. In the preliminary analysis of the resulting 2DE profiles, 18 protein spots were found to be differentially expressed in cells treated with GTT. This observa-tion is confirmed by extending the analysis to a larger sample size. By studying the effects of GTT treatment on differential protein expression in HepG2 cells the underly-ing mechanisms involved in the antitumor activity of GTT may be elucidated.