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Hydrolysis of riboflavin in plants

Kumar, SA and Vaidyanathan, CS (1964) Hydrolysis of riboflavin in plants. In: Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 89 (1). pp. 127-136.

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Official URL: http://dx.doi.org/10.1016/0926-6569(64)90106-3

Abstract

The enzymic hydrolysis of riboflavin to lumichrome and ribitol by extracts of Crinum longifolium bulbs has been demonstrated. The enzyme was purified 48-fold by ZnSO4 treatment and ethanol fractionation, and concentrated by using Sephadex G-25. After establishing the stoichiometry of the reaction, the general properties of the purified enzyme were studied. The enzyme showed maximal activity at pH 7·5, and it had a requirement for reduced glutathione which could be replaced by cysteine or ascorbic acid. Mg2+ and Li+ activated the enzyme. The reaction was highly specific to riboflavin and was competitively inhibited by riboflavin 5′-phosphate.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Science.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 21 May 2010 10:41
Last Modified: 19 Sep 2010 06:07
URI: http://eprints.iisc.ernet.in/id/eprint/28000

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