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Use of differential dye-ligand chromatography with affinity elution for enzyme purification: 2-Keto-3-deoxy-6-phosphogluconate aldolase from Zymomonas mobilis

✍ Scribed by R.K. Scopes

Publisher: Elsevier Science
Year: 1984
Tongue: English
Weight: 449 KB
Volume: 136
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(84)90256-2

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✦ Synopsis

2-Keto-3-deoxy-6-phosphogluconate aldolase (EC 4.1.2.14) has been isolated from extracts of Zymomonas mobilis using differential dye-ligand chromatography and affinity elution with product/product analog. The one-step procedure gives an enzyme with specific activity 600 units mg-1. Only 1 out of 47 dyes, Procion Yellow MX-GR, bound the enzyme completely in 20 mM phosphate buffer, pH 6.5. A column of Navy HE-R adsorbent was used first to remove most of the potentially adsorbing proteins.

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Use of differential dye-ligand chromatography with affinity elution for enzyme purification: 6-Phosphogluconate dehydratase from Zymomonas mobilis

✍ R.K. Scopes; K. Griffiths-Smith 📂 Article 📅 1984 🏛 Elsevier Science 🌐 English ⚖ 404 KB

Using differential dye-ligand chromatography and affinity elution with a substrate analog, 6-phosphogluconate dehydratase (EC 4.2.1.12) has been isolated from extracts of Zymomonas mobilis in a one-step procedure with 50% recovery. The specific activity of freshly isolated enzyme was 245 units mg-1.