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J. Biochem, 1984, Vol. 95, No. 6 1633-1644
© 1984 Japanese Biochemical Society

research-article

Characterization of Hen Egg White- and Yolk-Riboflavin Binding Proteins and Amino Acid Sequence of Egg White-Riboflavin Binding Protein

Yasuki HAMAZUME, Tomohiro MEGA and Tokuji IKENAKA

Department of Chemistry, Osaka University College of Science Toyonaka, Osaka 560

White- and Yolk-riboflavin binding proteins were isolated from hen eggs, and characterized as to their chemical properties. White- and Yolk-RBPs had almost same amino acid compositions except for glutamic acid, but their carbohydrate compositions were different from each other.

The complete amino acid sequence of White-RBP was determined by conventional methods. White-RBP comprised 219 amino acid residues, and the amino- terminus was pyroglutamic acid (pyrrolidonecarboxylic acid). Two amino acids, lysine and asparagine, were found at the fourteenth residue from the amino-terminus. Carbohydrate chains were linked to asparagine residues at positions 36 and 147.

Both White- and Yolk-RBPs were phosphorylated. In White-RBP either six or seven of nine serine residues between Ser(185) and Ser(197) were phosphorylated. The amino acid sequences around phosphoserines showed that phosphorylation might occur at a serine residue in one of the following sequences; Ser-X-Glu or Ser-X-Ser(P).


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