Positions of disulfide bonds in riboflavin-binding protein of hen egg white.
Riboflavin-binding protein of hen egg white (egg-white RBP) comprised 219 amino acid residues and nine disulfide bonds. To identify the locations of these bonds, the native protein was oxidized with cyanogen bromide and digested with trypsin, thermolysin, and Staphylococcus aureus V8 protease. The cystine-containing peptides were isolated by HPLC. Amino acid analyses and amino acid sequence analyses of the reduced pyridylethylated derivatives of the cystine peptides showed that seven of the disulfide bonds were as follows: Cys(24)-Cys(73), Cys(57)-Cys(138), Cys(64)-Cys(110), Cys(99)-Cys(169), Cys(116)-Cys(134), Cys(103)-Cys(152), Cys(167)-Cys(202). The other two disulfide bonds were either Cys(5)-Cys(32) and Cys(33)-Cys(77) or Cys(5)-Cys(33) and Cys(32)-Cys(77).
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002352:Carrier Proteins / Q000032:analysis*; D002645:Chickens; D003488:Cyanogen Bromide; D004220:Disulfides / Q000032:analysis*; D004529:Egg White / Q000032:analysis*; D006868:Hydrolysis; D026901:Membrane Transport Proteins; D010084:Oxidation-Reduction; D010455:Peptides / Q000032:analysis; D011487:Protein Conformation; D014357:Trypsin
D000596:Amino Acids; D002352:Carrier Proteins; D004220:Disulfides; D026901:Membrane Transport Proteins; D010455:Peptides; C019079:riboflavin-binding protein; D014357:Trypsin; D003488:Cyanogen Bromide