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Acta Alimentaria
Authors:
G. Gulyás
,
L. Czeglédi
,
B. Béri
,
S. Harangi
,
E. Csősz
,
Z. Szabó
,
T. Janáky
, and
A. Jávor

The aim of this study was to investigate the differences in the proteome patterns of musculus longissimus dorsi between Charolais bulls slaughtered at 500 kg and 700 kg live weight using two-dimensional difference in gel electrophoresis (2D-DIGE) and liquid chromatography-mass spectrometry (LC-MS). Three hundred fifty protein spots were visualised on gels of which 10 showed different expression levels (P<0.05) between groups. After mass spectrometric analysis of spots, beta-enolase (ENO3) in five different spots, alpha-enolase (ENO1), triosephosphate isomerase (TPI1) in two different spots, alpha-actin (ACTA1), and heat shock protein beta-1 (HSPB1) were identified. ENO3, ENO1, TPI1, and ACTA1 had higher expression levels in bulls of 700 kg live weight group. ENO3, ENO1, and TPI1 are involved in energy metabolism, while ACTA1 is a structure protein in skeletal muscle. Up-regulation of heat shock protein beta-1 (HSPB1), which protein is reported to have correlation with tenderness, was observed in 500 kg weight group. Our result demonstrates that proteomic tools are useful in identifying markers associated with muscle development.

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