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Purification of the epstein-barr-virus c3d complement receptor of human lymphocytes-b - antigenic and functional-properties of the purified protein

Academic Article
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Overview

authors

  • Nemerow, Glen
  • Siaw, M. F. E.
  • Cooper, N. R.

publication date

  • May 1986

journal

  • Journal of Virology  Journal

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.

subject areas

  • B-Lymphocytes
  • Cell Line
  • Chromatography, Affinity
  • Complement C3
  • Complement C3d
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes
  • Herpesvirus 4, Human
  • Humans
  • Molecular Weight
  • Receptors, Complement
  • Receptors, Complement 3d
  • Receptors, Virus
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Identity

PubMed Central ID

  • PMC252969

International Standard Serial Number (ISSN)

  • 0022-538X

PubMed ID

  • 2422399
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Additional Document Info

start page

  • 709

end page

  • 712

volume

  • 58

issue

  • 2

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