کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9886137 | 1537496 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Selenium binding to human hemoglobin via selenotrisulfide
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کلمات کلیدی
MALDI-TOFGSHRBCDTNBRPLCRed blood cells - سلولهای قرمز خون5,5′-dithiobis(2-nitrobenzoic acid) - 5،5'-dithiobis (2-nitrobenzoic acid)PEN - خودکارmatrix-assisted laser desorption ionization-time of flight - زمان یونیزاسیون لیزر جذب لیزر ماتریس-زمان پروازHemoglobin - هموگلوبینHuman hemoglobin - هموگلوبین انسانیDAN - وReversed-phase liquid chromatography - کروماتوگرافی مایع فاز معکوسred blood cell - گلبول قرمز، اریتروسیتGlutathione - گلوتاتیون
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Selenotrisulfide (e.g., glutathione selenotrisulfide (GSSeSG)) is an important intermediate in the metabolism of selenite. However, its reactivity with biological substances such as peptides and proteins in the subsequent metabolism is still far from clearly understood, because of its chemical instability under physiological conditions. Penicillamine (Pen) is capable of generating a chemically stable and isolatable selenotrisulfide, PenSSeSPen. To explore the metabolic fate of selenite in red blood cells (RBC), we investigated the reaction of selenotrisulfide with human hemoglobin (Hb) using PenSSeSPen as a model. PenSSeSPen rapidly reacted with Hb under physiological conditions. From the analysis of selenium binding using the Langmuir type binding equation, the apparent binding number of selenium per Hb tetramer almost corresponded to the number of reactive thiol groups of Hb. The thiol group blockade of Hb by iodoacetamide treatment completely inhibited the reaction of PenSSeSPen with Hb. In addition, MALDI-TOF mass spectrometric analysis of the selenium-bound Hb revealed that PenSSe moiety binds to the β subunits of Hb. Overall, the reaction of PenSSeSPen with Hb appears to involve the thiol exchange between Pen and the cysteine residues on the β subunit of Hb.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1723, Issues 1â3, 25 May 2005, Pages 215-220
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1723, Issues 1â3, 25 May 2005, Pages 215-220
نویسندگان
Mamoru Haratake, Katsuyoshi Fujimoto, Masahiro Ono, Morio Nakayama,