Isolation and Partial Characterization of a Murine Cell Surface Glycoprotein with Affinity for Exogenously Added β2‐Microglobulin

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Abstract
Exogenously added .beta.2-microglobulin (.beta.2m) binds to a variety of murine cell types. The receptor for .beta.2m was 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 than 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.
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