Purification of the Epstein-Barr virus/C3d complement receptor of human B lymphocytes: antigenic and functional properties of the purified protein

  • Nemerow G
  • Siaw M
  • Cooper N
26Citations
Citations of this article
9Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

The Epstein-Barr virus/C3d receptor (CR2) of human B lymphocytes was purified to homogeneity from Raji cells by immunoaffinity chromatography. The average yield of the 145-kilodalton receptor was 400 pmol (50 micrograms) per 10(10) cells, representing an approximate 75% recovery. The isolated 145-kilodalton protein was antigenically and functionally intact as it reacted with several anti-CR2 monoclonal antibodies and bound purified Epstein-Barr virus and C3d,g. These findings with the purified molecule provide an unequivocal demonstration of the dual receptor functions of this protein.

Cite

CITATION STYLE

APA

Nemerow, G. R., Siaw, M. F., & Cooper, N. R. (1986). Purification of the Epstein-Barr virus/C3d complement receptor of human B lymphocytes: antigenic and functional properties of the purified protein. Journal of Virology, 58(2), 709–712. https://doi.org/10.1128/jvi.58.2.709-712.1986

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free