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.
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