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Purification and characterization of glyceraldehyde-3-phosphate-dehydrogenase (GAPDH) from pea seeds

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Purification and characterization of glyceraldehyde-3-phosphate-dehydrogenase (GAPDH) from pea seeds
 
Creator Gani, Zahid
Boradia, Vishant Mahendra
Raghu Ram, Janaki
Suryavanshi, Prashant Mohan
Patil, Pravinkumar
Kumar, Santosh
Singh, Ranvir
Raje, Manoj
Raje, Chaaya Iyengar
 
Subject QR Microbiology
 
Description 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.
 
Publisher Academic Press
 
Date 2016
 
Type Article
PeerReviewed
 
Relation http://dx.doi.org/10.1016/j.pep.2016.06.014
http://crdd.osdd.net/open/1929/
 
Identifier 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