The purification of horseradish peroxidase by affinity chromatography on Sepharose-bound concanavalin A

Michael G. Brattain, Michael E. Marks, Thomas G. Pretlow

Research output: Contribution to journalArticle

25 Scopus citations

Abstract

This report describes the use of affinity chromatography on Sepharose-bound concanavalin A for the purification of horseradish peroxidase. Samples of horseradish peroxidase with A403:A280 ratios ranging from 0.62 to 2.45 were purified to A403:A280 ratios ranging from approximately 2.8 to 3.1 with the recovery of 73% or more of the enzymatic activity. Characterization of the purified horseradish peroxidase showed an increased enzymatic activity with respect to both absorbance at 403 nm and protein content.

Original languageEnglish (US)
Pages (from-to)346-352
Number of pages7
JournalAnalytical Biochemistry
Volume72
Issue number1-2
DOIs
StatePublished - May 7 1976

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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