Structural changes of rabbit myosin subfragment 1 altered by malonaldehyde, a byproduct of lipid oxidation.
Rabbit myosin subfragment 1 was allowed to react with malonaldehyde, a byproduct of lipid oxidation in a model system containing the subfragment 1 and malonaldehyde. The modified subfragment 1 was compared to the control, with use of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), circular dichorism (CD), Fourier transform infrared spectroscopy (FT-IR), and free amino group measurements. Both the modified and control samples were cleaved with cyanogen bromide (BrCN) treatment, and the BrCN fragments were analyzed by SDS-PAGE with tricine gel. Results from SDS-PAGE suggest that malonaldehyde causes cross-linking or polymerization of the protein during incubation. Malonaldehyde also reduced alpha-helix content (CD), increased random structure (FT-IR), and eliminated some beta-strand structure (FT-IR) in subfragment 1.
Li
S J
SJ
Department of Animal Sciences, University of California, Davis 95616, USA. sjlifoodscience@sprintmail.com
King
A J
AJ
D000818:Animals; D003488:Cyanogen Bromide; D015227:Lipid Peroxidation; D008315:Malondialdehyde / Q000737:chemistry*; D018482:Muscle, Skeletal / Q000737:chemistry; D015879:Myosin Subfragments / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D011817:Rabbits; D017550:Spectroscopy, Fourier Transform Infrared
D015879:Myosin Subfragments; D010446:Peptide Fragments; D008315:Malondialdehyde; D003488:Cyanogen Bromide