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Kinetics of the Different Susceptibilities of the Four Human Immunoglobulin G Subclasses to Proteolysis by Human Lysosomal Elastase
Author(s) -
BAICI A.,
KNÖPFEL M.,
FEHR K.,
SKVARIL F.,
BÖNI A.
Publication year - 1980
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1980.tb00039.x
Subject(s) - papain , immunoglobulin fab fragments , immunoglobulin fc fragments , proteolysis , chemistry , elastase , immunoglobulin g , microbiology and biotechnology , cleavage (geology) , antibody , monoclonal antibody , fragment crystallizable region , biochemistry , enzyme , biology , peptide sequence , receptor , immunology , gene , complementarity determining region , paleontology , fracture (geology)
Human lysosomal clastase cleaves human monoclonal IgG into components that closely resemble the fragments produced by papain digestion IgG1 produced Fab, Fe and Fab‐Fc fragments; cleavage of IgG2 produced Fab‐Fc, Fab and Fc fragments: IgG3 gave rise to almost pure Fab und Fch (Fc covalently Joined to the extended hinge region polypetide of IgG3). and from IgG4, F(ab) 2 , Fab and Fc fragments were recovered. The relative susceptibilities of the four human IgG subclasses to proteolytic attack by elastase were studied kinetically and showed the following decrease order of susceptibility: IgG3 >IgG1 >IgG2 >IgG4. The Fab fragment from papain digestion of IgG1 and the corresponding fragment from clastase digestion showed indistinguishable molecular weights and immunochemical identity