کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9886108 | 1537495 | 2005 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Glucose-derived Amadori compounds of glutathione
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کلمات کلیدی
mass unitsTMAGlcCDNBTCAGSHGSTGPXm.u.DTNBGSSG1-chloro-2,4-dinitrobenzene - 1-کلرو-2،4-دینیتروبنزنROS - ROStrichloroacetic acid - اسید ترشکلراکتیکtrimethylamine - ترتی الیامینAmadori compounds - ترکیبات آمادوریTCEP - ساکتGlutathione - گلوتاتیونglutathione (oxidized form) - گلوتاتیون (فرم اکسید شده)glutathione (reduced form) - گلوتاتیون (فرم کاهش یافته)glutathione-S-transferase - گلوتاتیون S-ترانسفرازglutathione reductase - گلوتاتیون ردوکتازglutathione peroxidase - گلوتاتیون پراکسیدازGlucose - گلوکزNon-enzymatic glycation - گلیسیری غیر آنزیمیReactive oxygen species - گونههای فعال اکسیژن
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Glucose-derived Amadori compounds of glutathione Glucose-derived Amadori compounds of glutathione](/preview/png/9886108.png)
چکیده انگلیسی
Under the chromatographic conditions used in these studies we observed time- and concentration-dependent formation of N-1-Deoxy-fructos-1-yl glutathione as the major glycation product formed in the mixtures of GSH with glucose. N-1-Deoxy-fructos-1-yl glutathione had a characteristic positively charged ion with m/z = 470 Th in its LC-MS spectra. Mixtures of glutathione disulfide and glucose generated two compounds: N-1-Deoxy-fructos-1-yl GSSG (m/z = 775 Th) as major adduct and bis di-N, Nâ²-1-Deoxy-fructos-1-yl GSSG (m/z = 937 Th) as the minor one. All three compounds showed a resonance signal at 55.2 ppm in the 13C-NMR spectra as C(1) methylene group of deoxyfructosyl, which represents direct evidence that they are Amadori compounds. All three compounds purified from GSSG/Glc or GSH/Glc mixtures also showed LC-MS/MS fragmentation patterns identical to those of the synthetically synthesized N-1-Deoxy-fructos-1-yl glutathione, N-1-Deoxy-fructos-1-yl GSSG and bis di-N, Nâ²-1-Deoxy-fructos-1-yl GSSG. N-1-Deoxy-fructos-1-yl glutathione was shown to be a poor substrate for glutathione peroxidase (6.7% of the enzyme's original specific activity) and glutathione-S-transferase (25.7% of the original enzyme's specific activity). Glutathione reductase failed to recycle the disulfide bond within the structure of di-substituted bis di-N, Nâ²-1-Deoxy-fructos-1-yl GSSG. It showed only 1% of the original enzyme's specific activity, but retained its ability to reduce the disulfide bond within the structure of N-1-Deoxy-fructos-1-yl GSSG by 57% of its original specific activity. Since the GSH concentration in diabetic lens is significantly decreased and the glucose concentration can increase 10-fold and higher, the formation of Amadori products of the different forms of glutathione with this monosaccharide may be favored under these conditions and could contribute to a lowering of glutathione levels and an increase of oxidative stress observed in diabetic lens.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1724, Issues 1â2, 20 June 2005, Pages 181-193
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1724, Issues 1â2, 20 June 2005, Pages 181-193
نویسندگان
Mikhail D. Linetsky, Ekaterina V. Shipova, Roy D. Legrand, Ognyan O. Argirov,