Positions of disulfide bonds in riboflavin-binding protein of hen egg white.

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… (More)

Topics

Figures and Tables

Sorry, we couldn't extract any figures or tables for this paper.

Slides referencing similar topics