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

✍ Scribed by Michael G. Brattain; Michael E. Marks; Thomas G. Pretlow II

Publisher: Elsevier Science
Year: 1976
Tongue: English
Weight: 426 KB
Volume: 72
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(76)90540-6

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✦ Synopsis

This report describes the use of affinity chromatography on Sepharose-bound concanavalin A for the purification of horseradish peroxidase. Samples of horseradish peroxidase with A .,03:A280 ratios ranging from 0.62 to 2.45 were purified to AIOa:AZSO 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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