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Affinity Chromatography of β 2 ‐Microglobulin from Human Lymphocytes on Concanavalin‐A‐Sepharose
Author(s) -
PLESNER T.
Publication year - 1976
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.1365-3083.1976.tb00249.x
Subject(s) - beta 2 microglobulin , concanavalin a , affinity chromatography , sepharose , radioimmunoassay , chemistry , chromatography , biochemistry , microbiology and biotechnology , biology , immunology , enzyme , in vitro
β 2 was extracted from human lymphocytes with nononic detergent and separated by affinity chromatography on concanavalin‐A‐Sepharose. The retarded part β 2 ‐micorglobulin is assumed to be associated with HLA antigens. Using a radioimmunoassay for β 2 ‐microglobulin, the average number of presumably free β 2 ‐microglobulin molecules and of presumably HLA‐associated β 2 ‐microglobulin molecules per lymphocyte was estimated to be 3.8 × 10 5 and 1.4 × 10 5 , respectively.