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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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
Publication:	Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects
Publisher:	Elsevier Science
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.ac.in/id/eprint/28000

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