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I had just made several hours worth of corrections on this article, and Firefox went belly-up on me (of course). Because of that, I am in no pleasant mood and will not likely be going through all that again for awhile. I will get around to fixing this article, and replacing all those beautiful external links, sometime later. Furthermore, as I have to include all the information (and around 20 times more) about GSTs in the introduction to my dissertation, I will not be entering anything under the GFDL (and/or the public domain) until I have published my dissertation and obtained a copyright on it. Sorry, but I can't put Wikipedia information in my intro and don't want to have one of my committee members read this article and accuse me of plagiarizing (myself). I'll slowly add more to the article as I find time. FMephit 18:17, 7 April 2006 (UTC)
The article title is not optimal - as can be read in (source at end - Mannervick et al.), the trivial name is Glutathione Tranferases, (without the S-). I suggest renaming this page, and creating a auto-redirect from the current page name to the new page, however I don't have the knowledge of how to do this, and don't want to break wikipedia! Thank you! B. R. Mannervik, P. G. Board, J. Hayes, I. Listowsky and W. R. Pearson, in Gluthione Transferases and Gamma-Glutamyl Transpeptidases, Elsevier Academic Press Inc, San Diego, 2005, vol. 401, pp. 1-8. Tom Meakin ( talk) 12:14, 15 January 2008 (UTC)
I should be able to improve and add to this page over the next few months. I just started a research project in this area and need something to do while I run gels! Pdcook ( talk) 14:56, 10 September 2009 (UTC)
Here it is: “Glutathione S-transferase can be added to a protein of interest to purify it from a solution of proteins. This is done by inserting the sequence of DNA that codes for glutathione S-transferase next to the sequence of DNA that codes for the protein of interest. Thus, after transcription and translation, the glutathione S-transferase protein and the protein of interest will be fused together in what is known as a fusion protein. Logically, the glutathione S-transferase protein has strong binding affinity for glutathione and scientists can add beads that are coated with glutathione to the protein mixture. As a result, the protein of interest that is attached to the glutathione S-transferase will stick to the beads, isolating the protein from the rest of the proteins in the solution. This is known as a pull-down assay. These beads can be obtained and then washed with free glutathione to detach the protein of interest from the beads, resulting in a purified protein. A drawback of this assay is that the protein of interest is stuck to the GST.”
Flemingrjf ( talk) 01:39, 23 April 2013 (UTC)
need adding it? -- —Preceding unsigned comment added by 24.248.198.18 ( talk) 17:52, 23 December 2009 (UTC)
Can someone who understand please clarify and change this sentence which I do not understand:
"GSTs catalyse the conjugation of reduced glutathione — via a sulfhydryl group — toelectrophilic centers on a wide variety of substrates."
Maybe there should be an article for "conjugate" (in this sense)? Nopedia ( talk) 14:18, 9 January 2013 (UTC)
BreCaitlin ( talk) 14:17, 30 April 2013 (UTC)
Best of luck editing the rest of your article. Gpruett2 ( talk) 20:55, 5 May 2013 (UTC)
Well done! Good luck with everything! Maximus155 ( talk) 19:26, 8 May 2013 (UTC)
Hi -- I posted a link in the External Links section that of this page that is apparently a COI. Apologies to Wikipedia, a site I have loved for years! I wat trying to post a GST scientific "methods and protocols" handbook offered by GE Life Sciences. The handbook doesn't require registration, so I thought it was good to add the discussion. Maybe the page editors can take a look at it and decide,...if it reeks too much of promotion it can come down. http://www.gelifesciences.com/gehcls_images/GELS/Related%20Content/Files/1314807262343/litdoc18115758_20140113001413.pdf — Preceding unsigned comment added by Lv131 ( talk • contribs) 21:51, 13 June 2014 (UTC)
![]() | Glutathione S-transferase received a peer review by Wikipedia editors, which is now archived. It may contain ideas you can use to improve this article. |
![]() | This article is rated Start-class on Wikipedia's
content assessment scale. It is of interest to the following WikiProjects: | |||||||||||||
|
![]() | This article links to one or more target anchors that no longer exist.
Please help fix the broken anchors. You can remove this template after fixing the problems. |
Reporting errors |
I had just made several hours worth of corrections on this article, and Firefox went belly-up on me (of course). Because of that, I am in no pleasant mood and will not likely be going through all that again for awhile. I will get around to fixing this article, and replacing all those beautiful external links, sometime later. Furthermore, as I have to include all the information (and around 20 times more) about GSTs in the introduction to my dissertation, I will not be entering anything under the GFDL (and/or the public domain) until I have published my dissertation and obtained a copyright on it. Sorry, but I can't put Wikipedia information in my intro and don't want to have one of my committee members read this article and accuse me of plagiarizing (myself). I'll slowly add more to the article as I find time. FMephit 18:17, 7 April 2006 (UTC)
The article title is not optimal - as can be read in (source at end - Mannervick et al.), the trivial name is Glutathione Tranferases, (without the S-). I suggest renaming this page, and creating a auto-redirect from the current page name to the new page, however I don't have the knowledge of how to do this, and don't want to break wikipedia! Thank you! B. R. Mannervik, P. G. Board, J. Hayes, I. Listowsky and W. R. Pearson, in Gluthione Transferases and Gamma-Glutamyl Transpeptidases, Elsevier Academic Press Inc, San Diego, 2005, vol. 401, pp. 1-8. Tom Meakin ( talk) 12:14, 15 January 2008 (UTC)
I should be able to improve and add to this page over the next few months. I just started a research project in this area and need something to do while I run gels! Pdcook ( talk) 14:56, 10 September 2009 (UTC)
Here it is: “Glutathione S-transferase can be added to a protein of interest to purify it from a solution of proteins. This is done by inserting the sequence of DNA that codes for glutathione S-transferase next to the sequence of DNA that codes for the protein of interest. Thus, after transcription and translation, the glutathione S-transferase protein and the protein of interest will be fused together in what is known as a fusion protein. Logically, the glutathione S-transferase protein has strong binding affinity for glutathione and scientists can add beads that are coated with glutathione to the protein mixture. As a result, the protein of interest that is attached to the glutathione S-transferase will stick to the beads, isolating the protein from the rest of the proteins in the solution. This is known as a pull-down assay. These beads can be obtained and then washed with free glutathione to detach the protein of interest from the beads, resulting in a purified protein. A drawback of this assay is that the protein of interest is stuck to the GST.”
Flemingrjf ( talk) 01:39, 23 April 2013 (UTC)
need adding it? -- —Preceding unsigned comment added by 24.248.198.18 ( talk) 17:52, 23 December 2009 (UTC)
Can someone who understand please clarify and change this sentence which I do not understand:
"GSTs catalyse the conjugation of reduced glutathione — via a sulfhydryl group — toelectrophilic centers on a wide variety of substrates."
Maybe there should be an article for "conjugate" (in this sense)? Nopedia ( talk) 14:18, 9 January 2013 (UTC)
BreCaitlin ( talk) 14:17, 30 April 2013 (UTC)
Best of luck editing the rest of your article. Gpruett2 ( talk) 20:55, 5 May 2013 (UTC)
Well done! Good luck with everything! Maximus155 ( talk) 19:26, 8 May 2013 (UTC)
Hi -- I posted a link in the External Links section that of this page that is apparently a COI. Apologies to Wikipedia, a site I have loved for years! I wat trying to post a GST scientific "methods and protocols" handbook offered by GE Life Sciences. The handbook doesn't require registration, so I thought it was good to add the discussion. Maybe the page editors can take a look at it and decide,...if it reeks too much of promotion it can come down. http://www.gelifesciences.com/gehcls_images/GELS/Related%20Content/Files/1314807262343/litdoc18115758_20140113001413.pdf — Preceding unsigned comment added by Lv131 ( talk • contribs) 21:51, 13 June 2014 (UTC)