Electrophoretic Separation of Proteins and Peptides in Bone Extract and Bone Extract Hydrolysates
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Abstract:
Bone extract (BE) and BE hydrolysate proteins and peptides were isolated and purified, and the differences in BE protein, bone protein, and muscle protein were compared. Bone protein and muscle protein were used as the controls, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to separate BE protein and BE hydrolyzed peptides. The effect of different running gel concentrations (5%, 7.5%, 10%, 15%) on the separation of BE protein, bone protein, and muscle protein was investigated. The results showed that bone protein and muscle protein were separated successfully, while BE protein was not separated by SDS-PAGE. In contrast, BE hydrolysate peptides were separated by N-Tris-(hydroxymethyl)-methylglycine gel electrophoresis. Analysis of the relationship between the electrophoresis migration ratio of BP and the running gel concentrations for SDS-PAGE revealed an extremely significant (R2≥0.996, p<0.01) correlation between the migration ratio and the running gel concentration. Combining this correlation with the correlation equation of the molecular weight of the proteins and the migration ratio allows us to choose the running gel concentration according to the molecular weight of a protein, or in turn to calculate the molecular weight of a protein based on its migration ratio.
