Abstract
1. A method is described for preparing pure samples of 19s gamma-globulin (IgM) from normal human serum by using successive steps of dialysis, density-gradient ultracentrifugation, chromatography on DEAE-cellulose, and gel filtration on Sephadex G-200. The yield of IgM (20-25mg./100ml. of serum) was equivalent to about one-quarter of that present in normal serum. 2. Analysis of the separated peptide chains of normal IgM and IgG (7s gamma-globulin) showed considerable differences in the amino acid composition of A chains from the two proteins; their respective B chains, on the other hand, were similar in composition. The carbohydrate of both proteins is confined almost entirely to the A chains; the IgM A chain contains about four times as much carbohydrate as the IgG A chain. 3. These findings support the view that the different classes of human immunoglobulin have B chains that are identical and A chains that are chemically distinct.
Keywords
BIOCHEMISTRY
CHROMATOGRAPHY
DIALYSIS
GAMMA GLOBULIN
19S
GEL FILTRATION
IMMUNOCHEMISTRY
IMMUNOELECTROPHORESIS
PEPTIDES
ULTRACENTRIFUGATION
MeSH Terms
Amino Acids
Biochemical Phenomena
Biochemistry
Chromatography
Chromatography, Gel
Dialysis
Humans
Immunochemistry
Immunoelectrophoresis
Immunoglobulin G
Immunoglobulin M
Peptides
Proteins
Renal Dialysis
Ultracentrifugation
gamma-Globulins
Chemicals
Amino Acids
Immunoglobulin G
Immunoglobulin M
Peptides
Proteins
gamma-Globulins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
CHAPLIN H
COHEN S
PRESS E M
References (28)
28 references, click to expand
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