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.
![[img]](http://eprints.iisc.ernet.in/style/images/fileicons/application_pdf.png) |
PDF
18.pdf - Published Version Restricted to Registered users only Download (443Kb) | Request a copy |
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 |
Actions (login required)
 |
View Item |
