کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8881570 | 1624884 | 2017 | 29 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Disulphide structure of high-molecular-weight (HMW-) gliadins as affected by terminators
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کلمات کلیدی
TRISGPCLMWHMWMRMTFAETDNEMICIDESIWheat flour - آرد گندمCollision-induced dissociation - اختلاف ناشی از برخوردTrifluoroacetic acid - اسید TrifluoroaceticElectron transfer dissociation - انحلال انتقال الکترونDisulphide bonds - اوراق قرضه disulfideTerminators - ترمیناتورهاRoom temperature - دمای اتاقDisulphide - دیسپولیدTCEP - ساکتMass spectrometry - طیف سنجی جرمیReversed-phase - فاز معکوسEIC - مهندسانmultiple reaction monitoring - نظارت چندگانه چندگانهglutenin subunit - واحد گلوتنینHigh-molecular-weight - وزن مولکولی بالاlow-molecular-weight - وزن کم مولکولیpolymerisation - پلیمریزاسیونliquid chromatography - کروماتوگرافی مایعhigh-performance liquid chromatography - کروماتوگرافی مایعی کاراHPLC - کروماتوگرافی مایعی کاراgel-permeation chromatography - کروماتوگرافی نفوذ ژلextracted ion chromatogram - کروماتوگرافی یون استخراج شدهelectrospray ionisation - یونیزاسیون الکترو اسپری
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
علوم زراعت و اصلاح نباتات
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چکیده انگلیسی
This study aimed at elucidating SS-bonds of HMW-gliadins (HGL) from wheat with the focus on terminators of glutenin polymerisation. HGL from wheat flour extracts non-treated or treated with the S-alkylation reagent N-ethylmaleinimide (NEMI) were compared. HGL from wheat flour Akteur were isolated, hydrolysed with thermolysin and the resulting peptides pre-separated by gel permeation chromatography and analysed by liquid chromatography/mass-spectrometry using alternating electron transfer dissociation/collision-induced dissociation. Altogether, 22 and 28 SS-peptides from samples without and with NEMI treatment, respectively, were identified. Twenty-six peptides included standard SS-bonds of α- and γ-gliadins, high-molecular-weight and low-molecular-weight glutenin subunits. Eleven SS-bonds were identified for the first time. Fifteen peptides unique to HGL contained cysteine residues from gliadins with an odd number of cysteines (Ï5-, α- and γ-gliadins). Thus, gliadins with an odd number of cysteines, glutathione and cysteine had acted as terminators of glutenin polymerisation. Decisive differences between samples without and with NEMI treatment were not obvious showing that the termination of polymerisation was already completed in the flour. The two HGL samples, however, were different in the majority of ten peptides that included disulphide-linked low-molecular-weight (LMW) thiols such as glutathione and cysteine with the former being enriched in the non-treated HGL-sample.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Cereal Science - Volume 78, November 2017, Pages 66-74
Journal: Journal of Cereal Science - Volume 78, November 2017, Pages 66-74
نویسندگان
Markus Schmid, Herbert Wieser, Peter Koehler,