Abstract
Proteins and peptides in bovine milk and colostrum were separated by two-dimensional gel electrophoresis (2-DE). The proteins were separated in the first dimension by isoelectric focusing in the pH ranges 4–7 and 6–11, and in the second dimension by sodium dodecyl sulphate polyacrylamide gel electrophoresis on 12.5% T homogeneous gels. The peptides were separated in the pH range 3–10 in the first dimension, while 15% T homogeneous gels were used in the second dimension. 2-DE evaluation of samples with various somatic cell counts showed an increased number of peptides with increased cell count. 2-DE analysis of samples heated at 65 and 85 °C for 30 min showed a decrease in the number of proteins and peptides with increased temperature. Colostrum exhibited a peptide pattern in which the intensity and number of spots decreased with time postpartum. These results show that 2-DE is a useful tool to detect variations of proteins and peptides in milk.
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