Isolation and partial characterization of a murine cell surface glycoprotein with affinity for exogenously added beta 2-microglubulin.

Abstract:

:Exogenously added beta 2-microglobulin (beta 2m) binds to a variety of murine cell types. The 'receptor' for beta 2m has been isolated. The purified 'receptor' comprised a 48,000-dalton chain and occasionally a 25,000-dalton component. Direct crosslinking of beta 2m to the receptor on intact cells gave rise to a single 60,000-dalton beta 2m-'receptor' complex. The molecular characteristics of the 'receptor' were considerably changed on binding beta 2m. The size of the beta 2m-'receptor' complex was increased partly due to enhanced binding of deoxycholate. The 'receptor' was less easily degraded by proteases when beta 2m 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-2K, D or Ia antigens.

journal_name

Scand J Immunol

authors

Sege K,Peterson PA

doi

10.1111/j.1365-3083.1980.tb00014.x

subject

Has Abstract

pub_date

1980-01-01 00:00:00

pages

461-70

issue

5

eissn

0300-9475

issn

1365-3083

journal_volume

11

pub_type

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