کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8291981 | 1536478 | 2008 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of the complex of glutathione S-transferase pi and 1-cysteine peroxiredoxin
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Characterization of the complex of glutathione S-transferase pi and 1-cysteine peroxiredoxin Characterization of the complex of glutathione S-transferase pi and 1-cysteine peroxiredoxin](/preview/png/8291981.png)
چکیده انگلیسی
Glutathione S-transferase pi has been shown to reactivate 1-cysteine peroxiredoxin (1-Cys Prx) by formation of a complex [L.A. Ralat, Y. Manevich, A.B. Fisher, R.F. Colman, Biochemistry 45 (2006) 360-372]. A model of the complex was proposed based on the crystal structures of the two enzymes. We have now characterized the complex of GST pi/1-Cys Prx by determining the Mw of the complex, by measuring the catalytic activity of the GST pi monomer, and by identifying the interaction sites between GST pi and 1-Cys Prx. The Mw of the purified GST pi/1-Cys Prx complex is 50,200 at pH 8.0 in the presence of 2.5Â mM glutathione, as measured by light scattering, providing direct evidence that the active complex is a heterodimer composed of equimolar amounts of the two proteins. In the presence of 4Â M KBr, GST pi is dissociated to monomer and retains catalytic activity, but the Km value for GSH is increased substantially. To identify the peptides of GST pi that interact with 1-Cys Prx, GST pi was digested with V8 protease and the peptides were purified. The binding by 1-Cys Prx of each of four pure GST pi peptides (residues 41-85, 115-124, 131-163, and 164-197) was investigated by protein fluorescence titration. An apparent stoichiometry of 1Â mol/subunit 1-Cys Prx was measured for each peptide and the formation of the heterodimer is decreased when these peptides are included in the incubation mixture. These results support our proposed model of the heterodimer.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 474, Issue 1, 1 June 2008, Pages 109-118
Journal: Archives of Biochemistry and Biophysics - Volume 474, Issue 1, 1 June 2008, Pages 109-118
نویسندگان
Luis A. Ralat, Stephanie A. Misquitta, Yefim Manevich, Aron B. Fisher, Roberta F. Colman,