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Isolation of IgG3 from Normal Human Sera and from a Patient with Multiple Myeloma by Using Protein A‐Sepharose 4B
Author(s) -
HJELM H
Publication year - 1975
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.1365-3083.1975.tb02671.x
Subject(s) - sepharose , sodium dodecyl sulfate , ultracentrifuge , sephadex , chemistry , chromatography , affinity chromatography , polyacrylamide gel electrophoresis , gel electrophoresis , myeloma protein , microbiology and biotechnology , bence jones protein , antibody , biochemistry , gel permeation chromatography , subclass , biology , immunoglobulin light chain , enzyme , immunology , organic chemistry , polymer
Affinity chromatography of IgG on protein A‐Sepharose was used to isolate the human subclass IgG3 from normal serum and from a patient with multiple myeloma. The isolated material was purified by chromatography mi Sephadex G‐150 and characterized immunochemically Ultracentrifugation studies gave s° 20 values of about 6.30 for both normal and myeloma IgG3 Approximately 54 halfcystine residues per molecule of IgG3 were obtained as judged from amino acid analysts after performic acid oxidation of the proteins. Polyacrylamide gel electrophoresis in 0.1% sodium dodecyl sulfate of the isolated and reduced material resulted in two bands correspoding to molecular weights of approximately 23.000 and 56.000. respectively. The yield of normal human IgG3 represented 1%‐2% of the tout IgG.