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
Affinity chromatography of urate oxidase on 8-aminoxanthine-bound Sepharose
โ Scribed by Takafumi Watanabe; Tetsuya Suga
- Publisher
- Elsevier Science
- Year
- 1978
- Tongue
- English
- Weight
- 309 KB
- Volume
- 86
- Category
- Article
- ISSN
- 0003-2697
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โฆ Synopsis
An agarose derivative that is an affinity adsorbent for chromatography of mate oxidase was prepared by coupling X-aminoxanthine with epoxy-activated Sepharose 4B. This affinity adsorbent was stable in 0.1 M borate buffer(pH 10.0) at 4ยฐC since no decrease of effective ligand content in the gel was found for 5 months. Chromatography of crude urate oxidases prepared from bovine kidney, rat liver, and yeast on the affinity column resulted in 2-to 88-fold purifications.
๐ SIMILAR VOLUMES
The seeds of Griffonia simplicifolia contain a family of five isolectins (GS-I) (L. A. Murphy and I. J. Goldstein (1977) J. Biol. Chem. 252, 4739-4742) that bind with high affinity to glycoconjugates containing terminal nonreducing alpha-linked galactose residues. Here, we report that GS-I itself is