-
Views
-
Cite
Cite
Yasuki HAMAZUME, Tomohiro MEGA, Tokuji IKENAKA, Positions of Disulfide Bonds in Riboflavin Protein of Hen Egg White, The Journal of Biochemistry, Volume 101, Issue 1, January 1987, Pages 217–223, https://doi.org/10.1093/oxfordjournals.jbchem.a121894
- Share Icon Share
Abstract
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(l 10), Cys(99)-Cys(169), Cys(116)-Cys(134), Cys(103)-Cys(l52), 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).