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

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

doi:10.1016/0003-2697(76)90540-6

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

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

Eppley Institute for Cancer Research

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	346-352
Number of pages	7
Journal	Analytical Biochemistry
Volume	72
Issue number	1-2
DOIs	https://doi.org/10.1016/0003-2697(76)90540-6
State	Published - May 7 1976

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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AB - 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.

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