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Mild Chymotryptic Cleavage of Human IgG and its Major Subclasses
Author(s) -
GERRARD J.,
KOMVOPOULOS ATHENA,
TURNER M. W.
Publication year - 1974
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.1365-3083.1974.tb01228.x
Subject(s) - papain , chymotrypsin , cleavage (geology) , chemistry , size exclusion chromatography , microbiology and biotechnology , homology (biology) , immunoglobulin fab fragments , antibody , immunoglobulin g , gel electrophoresis , fragment crystallizable region , biochemistry , biology , trypsin , peptide sequence , enzyme , amino acid , immunology , gene , receptor , paleontology , fracture (geology) , complementarity determining region
The cleavage of pooled human IgG and IgG1, IgG2, and IgG3 myeloma proteins with α‐chymotrypsin has been studied. The products of digestion were analyzed by starch gel electrophoresis and fractionated by gel filtration, In addition to low molecular weight peptides an electrophoretically fast fragment from the Cγ3 homology region (ctFc') was detected in all cases. Pooled IgG, IgG1, and IgG3 proteins fielded appreciable amounts of an Fab‐like fragment. Finally, various high molecular weight fragments were released that appeared to resemble recently described fragments produced by papain. These were Fab/c‐like fragments from pooled IgG and IgG1, F(ab) 2 ‐like fragments from IgG2, and Fch‐like fragments from IgG3.