Sulfate-mediated affinity chromatography on NADP+-Sepharose of glutamate dehydrogenase from halophilic bacteria and of glucose-6-phosphate dehydrogenase from Escherichia coli

Leicht, W.

European Journal of Biochemistry 84(1): 133-139

1978


ISSN/ISBN: 0014-2956
PMID: 25766
DOI: 10.1111/j.1432-1033.1978.tb12149.x
Accession: 038984067

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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 (1M) 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 Escherichia coli. The effects are shown to be biospecific, suggesting that the strength of the interaction between protein and immobilized coenzymes is a function of the sulfate concentration.