Peptide mapping of ovoglobulins G2A and G2B in the domestic fowl

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Abstract
1. The purification of the two principal genetic variants of ovoglobulin G2 from egg‐whites is described. 2. Both ovoglobulin G2A and G2B had molecular weights of 47 ±2 kDa. They differed in their mobilities in non‐denaturing gels and in their isoelectric points, which were 4.9 and 5.3 for G2A and G2B respectively. 3. Peptide mapping using either chymotrypsin or V8 digestion revealed additional proteinase sensitive sites in ovoglobulin G2A. The results are consistent with one of the differences between the two ovoglobulins being the replacement of an acidic amino acid residue in G2A by a neutral residue in G2B.