Characterization of Hen Egg White- and Yolk-Riboflavin Binding Proteins and Amino Acid Sequence of Egg White-Riboflavin Binding Protein
- 1 June 1984
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 95 (6), 1633-1644
- https://doi.org/10.1093/oxfordjournals.jbchem.a134776
Abstract
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).Keywords
This publication has 14 references indexed in Scilit:
- On the Reactive Site of Streptomyces Subtilisin InhibitorThe Journal of Biochemistry, 1980
- Affinity chromatographic purification and comparison of riboflavin-binding proteins from laying hen liver and blood and from egg yolkComparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1980
- Rat incisor phosphoprotein. The nature of the phosphate and quantitation of the phosphoserine.Journal of Biological Chemistry, 1978
- Purification and Characterization of L-Pyrrolidonecarboxylate Peptidase from Bacillus amyloliquefaciensThe Journal of Biochemistry, 1978
- The Preparation and Enzymatic Hydrolysis of Reduced and S-Carboxymethylated ProteinsJournal of Biological Chemistry, 1963
- PREPARATION AND PROPERTIES OF RIBOFLAVIN FLAVOPROTEIN OF SOLUBLE FRACTION OF EGG YOLK1963
- Nonenzymatic Cleavage of Peptide Bonds: The Methionine Residues in Bovine Pancreatic RibonucleaseJournal of Biological Chemistry, 1962
- The Flavoprotein-Apoprotein System of Egg WhiteJournal of Biological Chemistry, 1959
- ANALYSIS, FRACTIONATION, AND PURIFICATION OF EGG WHITE PROTEINS WITH CELLULOSE-CATION EXCHANGERJournal of Biological Chemistry, 1958
- The disulphide bonds of insulinBiochemical Journal, 1955