Affinity chromatography purification of erythrocyte membrane proteins after selective labeling with trinitrobenzene sodium sulfonate

Guido Tarone, Maria Prat, Paolo M. Comoglio

Research output: Contribution to journalArticlepeer-review

Abstract

2,4,6-Trinitrobenzene sodium sulfonate may be used, under appropriate conditions, for specific surface labeling of erythrocyte plasma membranes. Trinitrophenylated ghost proteins are easily purified by reverse immunoadsorption using rabbit anti-dinitrophenyl antibodies covalently linked to Sepharose 4B. The advantages of a method that permits selective labeling of membrane molecules with a hapten and their purification by affinity chromatography are obvious. The possible applications of such a method in the investigation of the composition of plasma membranes are discussed.

Original languageEnglish
Pages (from-to)214-221
Number of pages8
JournalBBA - Biomembranes
Volume311
Issue number2
DOIs
Publication statusPublished - Jun 22 1973

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Medicine(all)

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