Abstract
1. Detailed physical, chemical, and immunologic studies of a protein closely related to the Fc fragment and heavy chain of G immunoglobulin (IgG), and elaborated by a subject with a lymphoproliferative disorder are presented. 2. The protein, which has a molecular weight of 51,000, was cleaved into two half molecules by reduction and alkylation. 3. The protein has few if any of the antigenic determinants of the antigen-binding (Fab) papain fragment of IgG, and has a striking similarity in its antigenic properties to the Fc fragment. 4. Fingerprint patterns resemble those of the crystallizable (Fc) fragment, and lack several peptides found in the heavy chain. 5. These findings suggest that the Fc fragment may be a real structural unit of IgG, and raise the possibility of the existence of three different types of polypeptide chains in G immunoglobulin.
Keywords
AMINO ACIDS
BIOCHEMISTRY
BLOOD PROTEIN DISORDERS
BLOOD PROTEIN ELECTROPHORESIS
DIGESTION
GAMMA GLOBULIN
7S
GEL DIFFUSION TESTS
HEAVY CHAIN DISEASE
IMMUNOCHEMISTRY
IMMUNOELECTROPHORESIS
PAPAIN
PEPSIN
PEPTIDES
PRECIPITIN TESTS
PROTEINURIA
MeSH Terms
Amino Acids
Antigens
Biochemical Phenomena
Biochemistry
Blood Protein Disorders
Blood Protein Electrophoresis
Digestion
Heavy Chain Disease
Humans
Immunochemistry
Immunodiffusion
Immunoelectrophoresis
Immunoglobulin Fc Fragments
Immunoglobulin G
Molecular Weight
Papain
Pepsin A
Peptides
Precipitin Tests
Proteins
Proteinuria
gamma-Globulins
Chemicals
Amino Acids
Antigens
Immunoglobulin Fc Fragments
Immunoglobulin G
Peptides
Proteins
gamma-Globulins
Papain
Pepsin A
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
FRANKLIN E C
References (22)
22 references, click to expand
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