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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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|
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