title: Structural characterization of immunoglobulin G using time-dependent disulfide bond reduction.
abstract: Time-dependent reduction of the disulfide bonds of immunoglobulin G (IgG) using dithiothreitol (DTT) was used to characterize the structure of IgG. After treatment with DTT, gel electrophoresis was used to separate the resulting IgG fragments, which were subsequently quantified. Using this approach, the disulfide bond between a light chain and a heavy chain was determined to be cleaved faster than the disulfide bonds between two heavy chains.
authors.affiliation: Department of Chemistry, Chungnam National University, Daejeon 305-764, South Korea.
authors.forename: Jangmi
authors.initials: J
authors.lastname: Hong
authors.forename: Aera
authors.initials: A
authors.lastname: Lee
authors.forename: Hyesun
authors.initials: H
authors.lastname: Han
authors.forename: Jeongkwon
authors.initials: J
authors.lastname: Kim
mesh_terms: D004220:Disulfides / Q000737:chemistry*; D004229:Dithiothreitol / Q000737:chemistry; D007074:Immunoglobulin G / Q000737:chemistry*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013696:Temperature
chemical_list: D004220:Disulfides; D007074:Immunoglobulin G; D004229:Dithiothreitol