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. 1981 Jul 1;197(1):227–232. doi: 10.1042/bj1970227

Plant flavokinase. Affinity-chromatographic procedure for the purification of the enzyme from mung-bean (Phaseolus aureus) seeds and conformational changes on its interaction with orthophosphate.

J Sobhanaditya, N A Rao
PMCID: PMC1163074  PMID: 6274324

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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