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) |
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Pages (from-to) | 346-352 |
Number of pages | 7 |
Journal | Analytical Biochemistry |
Volume | 72 |
Issue number | 1-2 |
DOIs | |
State | Published - May 7 1976 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology