VDAC Properties are influenced by the source of its Purification

Please use this identifier to cite or link to this item: http://tdudspace.texicon.in:8080/jspui/handle/123456789/261

Full metadata record

DC Field	Value	Language
dc.contributor.author	Dubey, Ashvini K	-
dc.contributor.author	Godbole, Ashwini	-
dc.contributor.author	Srinivasan, Sujitha	-
dc.contributor.author	Mathew, M.K.	-
dc.date.accessioned	2023-04-20T10:06:38Z	-
dc.date.available	2023-04-20T10:06:38Z	-
dc.date.issued	2014-08	-
dc.identifier.uri	http://tdudspace.texicon.in:8080/jspui/handle/123456789/261	-
dc.description.abstract	The Voltage Dependent Anion-Selective Channel (VDAC), the most abundant protein of the outer mitochondrial membrane (OMM), forms the major conduit for metabolite transport across this membrane. It has also been shown to be involved in cell death signalling through interaction with other proteins like Hexokinase and by mediating release of apoptogenic proteins like cyt c from mitochondria. As in case of other channel proteins, functional characterization of purified reconstituted protein by using electrophysiological techniques can be used in development of VDAC targeted drugs. Here we report electrophysiological properties of VDACs (one of the target for cancerous cells) purified from different sources.	en_US
dc.language.iso	en	en_US
dc.publisher	International Journal of Pharmacy and Pharmaceutical Sciences	en_US
dc.subject	VDAC	en_US
dc.subject	Mitochondria	en_US
dc.subject	BLM	en_US
dc.subject	Bacterial expression	en_US
dc.subject	Purification.	en_US
dc.title	VDAC Properties are influenced by the source of its Purification	en_US
dc.type	Article	en_US
Appears in Collections:	Faculty Publications

Files in This Item:

File	Description	Size	Format
IJPPS VDAC source.pdf Restricted Access		380.7 kB	Adobe PDF	View/Open Request a copy