Gani, Zahid and Boradia, Vishant Mahendra and Raghu Ram, Janaki and Suryavanshi, Prashant Mohan and Patil, Pravinkumar and Kumar, Santosh and Singh, Ranvir and Raje, Manoj and Raje, Chaaya Iyengar (2016) Purification and characterization of glyceraldehyde-3-phosphate-dehydrogenase (GAPDH) from pea seeds. Protein Expression and Purification, 127. pp. 22-27. ISSN 10465928
Full text not available from this repository. (Request a copy)Abstract
Glyceraldehyde-3-phosphate dehydrogenase [GAPDH, NAD + oxidoreductase (phosphorylating) 1.2.1.12] catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate coupled with the reduction of NAD(+) to NADH. In addition to its role in glycolysis, this enzyme has numerous alternate functions, in both prokaryotes and eukaryotes. In plants, additional functions have been reported from multiple species including Pisum sativum. A recent study has identified that GAPDH may play an important role in seed ageing and programmed cell death. Despite this the existing purification protocols are almost 40 years old, and only partial characterization of the enzyme has been reported. In the current study, we report a modified method for purification of enzymatically active pea seed GAPDH along with the characterization of the enzyme. Using 2D gel electrophoresis our study also demonstrates that pea seeds contain four isoforms of NAD(+) dependent GAPDH.
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright of this article belongs to Academic Press. |
| Uncontrolled Keywords: | Characterization; Glyceraldehyde-3-phosphate dehydrogenase; NAD(+) specific; Pea seed; Purification |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 27 Mar 2018 03:19 |
| Last Modified: | 27 Mar 2018 03:19 |
| URI: | http://crdd.osdd.net/open/id/eprint/1929 |
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