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Affinity-Chromatographic Procedure For The Purification Of The Enzyme From Mung-Bean (Phaseolus, Aureus) Seeds And Conformational-Changes On Its Interaction With Ortho-Phosphate

Sobhanaditya, J and Rao, NA (1981) Affinity-Chromatographic Procedure For The Purification Of The Enzyme From Mung-Bean (Phaseolus, Aureus) Seeds And Conformational-Changes On Its Interaction With Ortho-Phosphate. In: Biochemical Journal, 197 (1). pp. 227-232.

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Abstract

Flavokinase was purified, for the first time from a plant source [mung bean (Phaseolus aureus)] by affinity chromatography in the presence of orthophosphate and by using C-8 ATP-agarose (ATP linked through the C-8 position to beaded agarose), Cibacron Blue and riboflavin--Sepharoses. An altered substrates-saturation pattern was observed in the presence of K2HPO4. The conformational changes of the enzyme in the presence of K2HPO4 were monitored by fluorescence spectroscopy. These results highlight the regulatory nature of this enzyme.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Portland Press.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 08 Sep 2011 11:47
Last Modified: 08 Sep 2011 11:47
URI: http://eprints.iisc.ernet.in/id/eprint/40372

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