کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10738910 | 1046842 | 2005 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A new sensitive assay reveals that hemoglobin is oxidatively modified in vivo
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کلمات کلیدی
DTNB(Z)-1-[2-(2-aminoethyl)-N-(2-ammonioethyl)amino]diazen-1-ium-1,2-diolatetGSHTFAGSSGGSHN-ethylmaleimideTCAPBSMALDI-TOF5,5′-dithiobis(2-nitrobenzoic acid) - 5،5'-dithiobis (2-nitrobenzoic acid)DETA/NO - DETA / NOTrifluoroacetic acid - اسید Trifluoroacetictrichloroacetic acid - اسید ترشکلراکتیکOxidative modification - اصلاح اکسیداتیوANH - انگلستانAssay - تستOxidative stress - تنش اکسیداتیوBlood substitute - جایگزین خونFree radical - رادیکالهای آزاد metHb - مت هابmethemoglobin - متهموگلوبینPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریMyoglobin - میوگلوبینNEM - نهHemoglobin - هموگلوبینAcute Normovolemic Hemodilution - هومیوپاتی Normovolemic حادexercise - ورزشPeroxide - پراکسیدreduced glutathione - کاهش گلوتاتیونChlorin - کلرینoxidised glutathione - گلوتاتیون اکسید شدهtotal glutathione - گلوتاتیون کل
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
Free radical formation in heme proteins is recognised as a factor in mediating the toxicity of peroxides in oxidative stress. As well as initiating free radical damage, heme proteins damage themselves. Under extreme conditions, where oxidative stress and low pH coincide (e.g., myoglobin in the kidney following rhabdomyolysis and hemoglobin in the CSF subsequent to subarachnoid hemorrhage), peroxide can induce covalent heme to protein cross-linking. In this paper we show that, even at neutral pH, the heme in hemoglobin is covalently modified by oxidation. The product, which we term OxHm, is a “green heme” iron chlorin with a distinct optical spectrum. OxHm formation can be quantitatively prevented by reductants of ferryl iron, e.g., ascorbate. We have developed a simple, robust, and reproducible HPLC assay to study the extent of OxHm formation in the red cell in vivo. We show that hemoglobin is oxidatively damaged even in normal blood; approximately 1 in 2000 heme groups exist as OxHm in the steady state. We used a simple model (physical exercise) to demonstrate that OxHm increases significantly during acute oxidative stress. The exercise-induced increase is short-lived, suggesting the existence of an active mechanism for repairing or removing the damaged heme proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Free Radical Biology and Medicine - Volume 39, Issue 9, 1 November 2005, Pages 1216-1228
Journal: Free Radical Biology and Medicine - Volume 39, Issue 9, 1 November 2005, Pages 1216-1228
نویسندگان
Niels B.J. Vollaard, Brandon J. Reeder, Jerry P. Shearman, Patrick Menu, Michael T. Wilson, Chris E. Cooper,