title: Unique features of monoclonal IgG2b in the cleavage reaction with pepsin.
abstract: Preparations of IgG2b purified from several mouse hybridoma clones were highly susceptible, compared to other subclasses, to peptic digestion under conditions usually used to prepare F (ab')2 fragments. Analyses of the digestion products revealed that no F (ab')2 was produced and that the main product was a Fab-like fragment. Demonstration of the hinge disulfides in the Fc portion clearly indicated that in IgG2b the primary peptic cleavage occurs on the NH2-terminal side of the inter-heavy chain disulfide bridge. The resulting Fab failed to bind with antigen, suggesting the importance of the CH1-hinge region in maintaining the native conformation of the antigen-binding site.
authors.affiliation: Department of Orthopedic Surgery, Okayama University Medical School, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Sumii
authors.forename: K
authors.initials: K
authors.lastname: Tsutsui
authors.forename: M
authors.initials: M
authors.lastname: Hatsushika
authors.forename: H
authors.initials: H
authors.lastname: Inoue
authors.forename: G
authors.initials: G
authors.lastname: Tanabe
authors.forename: T
authors.initials: T
authors.lastname: Oda
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000032:analysis*; D007140:Immunoglobulin Fab Fragments / Q000032:analysis*; D007074:Immunoglobulin G / Q000032:analysis*; D066298:In Vitro Techniques; D051379:Mice; D010434:Pepsin A
chemical_list: D000911:Antibodies, Monoclonal; D007140:Immunoglobulin Fab Fragments; D007074:Immunoglobulin G; D010434:Pepsin A