Premium
Isolation of Fab and Fc Fragments from a Plasmin‐Treated Human Immunoglobulin by High‐Speed Gel Filtration on TSK G3000SW and G3000SWG
Author(s) -
Watabe S.,
Takada K.,
Shitori Y.,
Hashimoto K.
Publication year - 1985
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1985.tb00138.x
Subject(s) - plasmin , isolation (microbiology) , antibody , size exclusion chromatography , immunoglobulin g , chemistry , chromatography , filtration (mathematics) , immunology , microbiology and biotechnology , medicine , biology , biochemistry , enzyme , mathematics , statistics
A method is described for isolating intact 7S IgG, Fab and Fc fragments from a plasmin‐treated immunoglobulin by high‐speed gel filtration on a TSK G3000SW or G3000SWG column. The isolated 7S IgG, Fab and Fc fragments reacted with antihuman IgG, Fab and Fc antiserum, respectively, in both Ouchterlony's double immunodiffusion and immunoelectrophoresis. Each of the Fab and Fc fragments formed a single precipitation line, demonstrating their homogeneity. Anticomplementary activities of intact 7S IgG, Fab and Fc fragments were 2.5,≤10 and 2.5 mg protein/ml to inhibit 2 units of CH 50 , respectively, and the diphtheria antitoxin contents were 2.1, 6.0 and 1.5 IU/150 mg protein, respectively. The molecular composition of plasmin‐treated immunoglobulin as determined by gel filtration on a TSK G3000SW column was as follows: 7S IgG 38.0±0.2%; Fab 42.6±0.1% and Fc fragment 19.3±0.1%.