کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10754901 | 1050361 | 2014 | 24 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Hormonogenic donor Tyr2522 of bovine thyroglobulin. Insight into preferential T3 formation at thyroglobulin carboxyl terminus at low iodination level
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کلمات کلیدی
TPCKDABITCES/MSBTGDehydroalanineHTGMTG3,5,3′-triiodothyronine - 3،5،3'-triiodothyronineSDS–PAGE - SDS-PAGEAChE - آهیAcetylcholinesterase - استیل کولین استرازElectrospray mass spectrometry - اسپکترومتری جرم الکترو اسپریDIT - اینmit - باTrypsin - تریپسینhuman thyroglobulin - تریگرولوبولین انسانیbovine thyroglobulin - تیروئلاگلولین گاوThyroglobulin - تیروگلوبولینThyroid hormone synthesis - سنتز هورمون تیروئیدMass spectrometry - طیف سنجی جرمی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
A tryptic fragment (b5TR,NR), encompassing residues 2515-2750, was isolated from a low-iodine (0.26% by mass) bovine thyroglobulin, by limited proteolysis with trypsin and preparative, continuous-elution SDS-PAGE. The fragment was digested with Asp-N endoproteinase and analyzed by reverse-phase HPLC electrospray ionization quadrupole time-of-flight mass spectrometry, revealing the formation of: 3-monoiodotyrosine and dehydroalanine from Tyr2522; 3-monoiodotyrosine from Tyr2555 and Tyr2569; 3-monoiodotyrosine and 3,5-diiodotyrosine from Tyr2748. The data presented document, by direct mass spectrometric identifications, efficient iodophenoxyl ring transfer from monoiodinated hormonogenic donor Tyr2522 and efficient mono- and diiodination of hormonogenic acceptor Tyr2748, under conditions which permitted only limited iodination of Tyr2555 and Tyr2569, in low-iodine bovine thyroglobulin. The present study thereby provides: (1) a rationale for the preferential synthesis of T3 at the carboxy-terminal end of thyroglobulin, at low iodination level; (2) confirmation for the presence of an interspecifically conserved hormonogenic donor site in the carboxy-terminal domain of thyroglobulin; (3) solution for a previous uncertainty, concerning the precise location of such donor site in bovine thyroglobulin.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 450, Issue 1, 18 July 2014, Pages 488-493
Journal: Biochemical and Biophysical Research Communications - Volume 450, Issue 1, 18 July 2014, Pages 488-493
نویسندگان
Giovanni Paolo Cetrangolo, Alessia Arcaro, Alessio Lepore, Maria Graf, Gianfranco Mamone, Pasquale Ferranti, Giuseppe Palumbo, Fabrizio Gentile,