Effect of reduction and alkylation on structure and function of rabbit IgG antibody-I. Effect on ability to activate complement depends on conditions of reduction
Johnson, B.A.; Hoffmann, L.G.
Molecular Immunology 18(3): 181-188
ISSN/ISBN: 0161-5890 PMID: 7266486 DOI: 10.1016/0161-5890(81)90084-5
Anaerobic reduction of rabbit Ig G antibody with either dithiothreitol at p H 8.0 or 2-mercaptoethanol at p H 5.0 results in the production of antibody molecules which lack haemolytic activity yet whose interchain disulfide bonds remain intact. Aerobic reduction with 2-mercaptoethanol results in more haemolytic activity than can be accounted for by the residual amount of Ab with intact interchain bonds. Taken together, these findings suggest that the interheavy chain disulfide bond in rabbit Ig G is not essential for interaction with complement but that an intraheavy chain bond is critical.