Abstract
A number of immunological methods have been employed to show that the small subunit of HL-A antigens, isolated either after papain treatment or after solubilization with detergent, is identical to beta(2)-microglobulin, a protein previously isolated from human urine and shown to be homologous in structure to constant region domains of immunoglobulins. Moreover, quantitative data indicate virtually total identity between the small subunit of HL-A antigens and beta(2)-microglobulin. Studies of the turnover of labeled HL-A antigens from the lymphocyte surface indicate that the two subunits turn over at similar rates, although only the small subunit could be detected in the culture medium. The significance of these observations is discussed.
MeSH Terms
Animals
Antigen-Antibody Reactions
Antigens, Neoplasm
Beta-Globulins
Cell Membrane/immunology
Chemical Phenomena
Chemistry
Electrophoresis
Epitopes
Gels
Hemolysis
Histocompatibility Antigens
Humans
Immunoglobulin Fragments
Isoelectric Focusing
Kinetics
Leukemia, Lymphoid/immunology
Lymphocytes/immunology
Peptide Fragments
Rabbits/immunology
Urea
Chemicals
Antigens, Neoplasm
Beta-Globulins
Epitopes
Gels
Histocompatibility Antigens
Immunoglobulin Fragments
Peptide Fragments
Urea
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Cresswell P
Springer T
Strominger J L
Turner M J
Grey H M
Kubo R T
References (17)
17 references, click to expand
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