کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10739342 | 1046872 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Rates of nitric oxide dissociation from hemoglobin
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کلمات کلیدی
PBSPDTCdithioerythritoloxyHbSNO-HbS-nitrosohemoglobindeoxyHbHBSinositol hexaphosphateIHPDTEHbNOElectron paramagnetic resonance - تشدید پارامغناطیس الکترونEPR - تشدید پارامغناطیس الکترونDissociation kinetics - جنبشی انحلالPhosphate buffered saline - فسفات بافر شورmetHb - مت هابmethemoglobin - متهموگلوبینNitric oxide - نیتریک اکسیدHemoglobin - هموگلوبینdeoxygenated hemoglobin - هموگلوبین deoxygenatedOxygenated hemoglobin - هموگلوبین اکسید شدهSickle cell hemoglobin - هموگلوبین سلول سقط
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
Nitric oxide (NO) plays a major role in human physiology and in many pathological states. Although oxyhemoglobin is known to destroy NO activity, NO activity can, in principle, be conserved through iron nitrosylation at vacant hemes. In order for this NO activity to be delivered, the NO must dissociate from the heme. Despite its study over the past few decades, our understanding of NO dissociation from hemoglobin is incomplete. In principle, there are at least four NO dissociation rates: kRα, kRβ, kTα, and kTβ, where the subscript refers to the quaternary state and the superscript to the hemoglobin chain. In the T-state, a proportion of the proximal histidine bonds break forming pentacoordinate α-nitrosyl hemoglobin. In vivo, α -nitrosyl hemoglobin predominates over β-nitrosyl hemoglobin. In this study we have used a fast NO trap, Fe(II)-proline-dithiocarbamate, to measure NO dissociation rates from hemoglobin. We have varied solution conditions so the rate of dissociation from pentacoordinate α -nitrosyl hemoglobin could be definitively measured for the first time; kTα = 4.2 ± 1.5 à 10â4 sâ1. We have also found that the fastest NO dissociation rate is on the order of 10â3 sâ1 and that NO dissociation from sickle cell hemoglobin is the same as that from normal adult hemoglobin.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Free Radical Biology and Medicine - Volume 39, Issue 2, 15 July 2005, Pages 145-151
Journal: Free Radical Biology and Medicine - Volume 39, Issue 2, 15 July 2005, Pages 145-151
نویسندگان
Fouad Azizi, Jerrold E. Kielbasa, Adedoyin M. Adeyiga, Rachel D. Maree, Matthew Frazier, Mamudu Yakubu, Howard Shields, S. Bruce King, Daniel B. Kim-Shapiro,