Biophysical investigation of thymoquinone binding to 'N' and 'B' isoforms of human serum albumin: exploring the interaction mechanism and radical scavenging activity1. Issue 24 (15th March 2015)

Record Type:: Journal Article
Title:: Biophysical investigation of thymoquinone binding to 'N' and 'B' isoforms of human serum albumin: exploring the interaction mechanism and radical scavenging activity1. Issue 24 (15th March 2015)
Main Title:: Biophysical investigation of thymoquinone binding to 'N' and 'B' isoforms of human serum albumin: exploring the interaction mechanism and radical scavenging activity1
Authors:: Ishtikhar, Mohd
Rabbani, Gulam
Khan, Shawez
Khan, Rizwan Hasan
Abstract:: <abstract abstract-type="toc"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <graphic position="anchor" id="ga" xlink:href="ark:/27927/pgj411dq7x" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" />Thymoquinone more strongly interacts with the 'N' isoform in comparison to the 'B' isoform of HSA and also increases its thermal stability but the antioxidant activity is significantly higher at the 'B' isoform of HSA.</p> </abstract>
Is Part Of:: RSC advances. Volume 5:Issue 24(2015)
Journal:: RSC advances
Issue:: Volume 5:Issue 24(2015)
Issue Display:: Volume 5, Issue 24 (2015)
Year:: 2015
Volume:: 5
Issue:: 24
Issue Sort Value:: 2015-0005-0024-0000
Page Start:: 18218
Page End:: 18232
Publication Date:: 2015-03-15
Subjects:: Chemistry -- Periodicals
540.5
Journal URLs:: http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗
DOI:: 10.1039/c4ra09892g ↗
Languages:: English
ISSNs:: 2046-2069
Deposit Type:: Legaldeposit
View Content:: Available online (eLD content is only available in our Reading Rooms) ↗
Physical Locations:: British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store
Ingest File:: 3336.xml