Sulfate‐Mediated Affinity Chromatography on NADP+ ‐Sepharose of Glutamate Dehydrogenase from Halophilic Bacteria and of Glucose‐6‐Phosphate Dehydrogenase from Escherichia coli
- 1 March 1978
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 84 (1) , 133-139
- https://doi.org/10.1111/j.1432-1033.1978.tb12149.x
Abstract
An improved synthesis of the 8-(6-aminohexyl)amino derivative of NADP+ is described for use in affinity chromatography. The binding of glutamate dehydrogenase isolated from halobacterium of the Dead Sea on a column of Sepharose linked to this NADP+ derivative could be drastically enhanced by addition of sulfate (1 M) and provided a tool for partially purifying the enzyme from a crude extract. A similar finding is reported for glucose-6-phosphate dehydrogenase in crude extracts of E.coli. The effects are biospecific, suggesting that the strength of the interaction between protein and immobilized coenzymes is a function of the sulfate concentration.This publication has 20 references indexed in Scilit:
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