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. 1989 Oct;22(4):281-5.
doi: 10.1016/0165-2478(89)90166-1.

Solubilization of human peripheral nerve Fc gamma receptors and purification of a functional 40 kDa receptor

C A Vedeler  1 , R Matre, E K Kristoffersen
Affiliations

Solubilization of human peripheral nerve Fc gamma receptors and purification of a functional 40 kDa receptor

C A Vedeler et al. Immunol Lett. 1989 Oct.

Abstract

Extracts from myelinated and unmyelinated nerves, prepared using Tris-HCl buffer with EDTA and ME, contained functionally active receptors for the Fc region of IgG (FcR). This was evident from the results obtained in indirect haemagglutination and rosette inhibition assays. Using a monoclonal antibody, a functional active 40-kDa FcR was purified from the nerve extracts. The receptor was a single-chained glycoprotein with low affinity for native IgG, apparently belonging to the FcRII family. In addition, peripheral nerve extracts contain FcR not recognised by the monoclonal antibody.

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