Structural characterization of immunoglobulin G using time-dependent disulfide bond reduction.
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.
Hong
Jangmi
J
Department of Chemistry, Chungnam National University, Daejeon 305-764, South Korea.
Lee
Aera
A
Han
Hyesun
H
Kim
Jeongkwon
J
D004220:Disulfides / Q000737:chemistry*; D004229:Dithiothreitol / Q000737:chemistry; D007074:Immunoglobulin G / Q000737:chemistry*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013696:Temperature
D004220:Disulfides; D007074:Immunoglobulin G; D004229:Dithiothreitol