SwePub
Sök i LIBRIS databas

  Extended search

id:"swepub:oai:DiVA.org:uu-127483"
 

Search: id:"swepub:oai:DiVA.org:uu-127483" > Single-nucleotide p...

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

Single-nucleotide polymorphic variants of human glutathione transferase T1-1 differ in stability and functional properties

Josephy, David (author)
Kent, Meredith (author)
Mannervik, Bengt (author)
Uppsala universitet,Institutionen för biokemi och organisk kemi
 (creator_code:org_t)
Elsevier BV, 2009
2009
English.
In: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861 .- 1096-0384. ; 490:1, s. 24-29
  • Journal article (peer-reviewed)
Abstract Subject headings
Close  
  • We have previously expressed hexa-histidine-tagged human glutathione transferase GST T1-1 at very high levels in an Escherichia coli lacZ mutagenicity assay strain. Ethylene dibromide (EDB), which is activated by GST T1-1, produces a potent response in the mutation assay. We have now constructed and expressed two SNP variants of wild-type GST T1-1:D141N and E173K. The EDB activation activities of both variant enzymes, as measured by the lacZ mutagenicity assay, are greatly reduced The D141N variant behaved similarly to the wild-type enzyme, in terms of expression level and specific activities for conjugation of glutathione with 1,2-epoxy-3-(p-nitrophenoxy)propane (EPNP), ethylene diiodide (EDI), and 4-nitrobenzyl chloride (NBCl), and for peroxidative detoxication of cumene hydroperoxide (CuOOH). In contrast, variant E173K is poorly expressed, has no detectable activity with EPNP, NBCl, or CuOOH, and has EDI activity much lower than that of the wild-type enzyme. The circular dichroism (CD) thermal denaturation profiles of the wild-type protein and variant D141N show a sharp two-state transition between native and denatured states. Variant E173K showed a very different profile, consistent with improper or incomplete protein folding. Our results show that SNP variants can give rise to GSTT1-1 proteins with significantly altered properties. (C) 2009 Elsevier Inc. All rights reserved.

Subject headings

NATURVETENSKAP  -- Biologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences (hsv//eng)

Keyword

Glutathione transferase
Single nucleotide polymorphism
Biology
Biologi

Publication and Content Type

ref (subject category)
art (subject category)

Find in a library

To the university's database

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

Find more in SwePub

By the author/editor
Josephy, David
Kent, Meredith
Mannervik, Bengt
About the subject
NATURAL SCIENCES
NATURAL SCIENCES
and Biological Scien ...
Articles in the publication
Archives of Bioc ...
By the university
Uppsala University

Search outside SwePub

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view