Purification and characterization of the riboflavin-binding protein from goose (Anser anser) egg yolk
1994
Stevens, L. | Nicol, K. | Kelly, S.M. | Scott, C. | Reid, J.S.G. | Price, N.C.
The riboflavin-binding protein, purified from goose egg yolk, is significantly larger than those previously isolated from other avian species. This is, in part, due to a larger polypeptide chain, but mainly to a much higher carbohydrate content, principally glucose and sialic acid. Approximately one-third of the glucose residues can be released by incubation with a mixture of exo-1,4-alpha- and exo-1,4-beta-D-glucosidases. The amino acid composition is similar to that of other riboflavin-binding proteins, but the peptide maps are distinct from those of domestic fowl. The goose egg yolk protein has a much higher proportion of beta-sheet than either domestic fowl or quail riboflavin-binding protein.
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