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Isolation and Partial Characterization of a Murine Cell Surface Glycoprotein with Affinity for Exogenously Added β 2 ‐Microglobulin
Author(s) -
SEGE K.,
PETERSON P. A.
Publication year - 1980
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.1365-3083.1980.tb00014.x
Subject(s) - receptor , beta 2 microglobulin , glycoprotein , cell surface receptor , antigen , proteases , microbiology and biotechnology , biochemistry , cell , biology , chemistry , enzyme , immunology
Exogenously added β 2 microglobulin (β 2 m) binds to a variety or murine cell types. The ‘receptor’ for β 2 m has been isolated. The purified ‘receptor’ comprised a 48,000‐dalton chain and occasionally a 25,000‐dalton component. Direct crosslinking of β 2 m to the receptor on intact cells gave rise to a single 60,000‐dalton β 2 m‐‘receptor’ complex. The molecular characteristics of the ‘receptor’ were considerably changed on binding β 2 m. The size of the β 2 m‐‘receptor’ complex was increased partly due to enhanced binding of deoxycholate. The ‘receptor’ was less easily degraded by proteases when β 2 m was bound then when free. The solubilized ‘receptor’ reacted with a heteroantiserum raised against H‐2K and D antigens but did not exhibit any alloantigenic determinants shared with H‐2 K, D or Ia antigens.