Abstract.
Denaturing polyacrylamide gel electrophoresis (SDS-PAGE) was used to separate and identify the proteins soluble in low ionic strength buffer that were extracted from Semimembranosus and Biceps femoris muscles from raw hams and after curing for 11 months. The samples analysed were taken from three white pig crosses produced by three different selective breeding enterprises: cross A (75% Duroc-25% Landrace), cross B (50% Duroc-25% Landrace-25% Large White) and cross C (75% Duroc-25% Landrace). The electrophoretic profiles for the two muscles from the raw hams were qualitatively similar, but the profiles for the muscles from the cured hams revealed changes in the electrophoretic bands in the range of 66–149 kDa. The relative concentrations of certain proteins differed in both the raw and cured hams from the three crosses. Curing resulted in the loss of electrophoretic bands, chiefly for the higher molecular weights; the appearance of new protein fragments, primarily in the range of 9–22 kDa, and quantitative variations in certain polypeptides.
Similar content being viewed by others
Author information
Authors and Affiliations
Additional information
Electronic Publication
Rights and permissions
About this article
Cite this article
Soriano Pérez, A., García Ruiz, A., Mariscal Contreras, C. et al. Separation and identification of sarcoplasmic proteins from hams from three white pig crosses containing Duroc. Eur Food Res Technol 216, 193–198 (2003). https://doi.org/10.1007/s00217-002-0633-8
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/s00217-002-0633-8