Hamazume Y, Mega T, Ikenaka T
J Biochem. 1984 Jun;95(6):1633-44. doi: 10.1093/oxfordjournals.jbchem.a134776.
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).
从鸡蛋中分离出蛋清和蛋黄核黄素结合蛋白，并对其化学性质进行了表征。除谷氨酸外，蛋清和蛋黄核黄素结合蛋白的氨基酸组成几乎相同，但它们的碳水化合物组成彼此不同。通过传统方法确定了蛋清核黄素结合蛋白的完整氨基酸序列。蛋清核黄素结合蛋白由219个氨基酸残基组成，氨基末端为焦谷氨酸（吡咯烷酮羧酸）。在距氨基末端第14个残基处发现了两个氨基酸，赖氨酸和天冬酰胺。碳水化合物链连接到第36和147位的天冬酰胺残基上。蛋清和蛋黄核黄素结合蛋白均被磷酸化。在蛋清核黄素结合蛋白中，Ser(185)和Ser(197)之间的九个丝氨酸残基中有六个或七个被磷酸化。磷酸丝氨酸周围的氨基酸序列表明，磷酸化可能发生在以下序列之一的丝氨酸残基上：Ser-X-Glu或Ser-X-Ser(P)。
