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 | |
| State | Published - May 7 1976 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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Cite this
Brattain, M. G., Marks, M. E., & Pretlow, T. G. (1976). The purification of horseradish peroxidase by affinity chromatography on Sepharose-bound concanavalin A. Analytical Biochemistry, 72(1-2), 346-352. https://doi.org/10.1016/0003-2697(76)90540-6