کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2018269 | 1067842 | 2007 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Immunodetection and immunolocalization of tryptophanins in oat (Avena sativa L.) seeds
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کلمات کلیدی
TrpCLSMDTTPuroindolinesAvena sativa L.PuroindolineLipid binding ProteinsSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدSodium dodecyl sulfate polyacrylamide gel electrophoresis - الکتروفورز ژل پلی اتیل آمید سدیم دودسیل سولفاتdithiothreitol - دیتیوتریتولconfocal laser scanning microscopy - میکروسکوپهای اسکن لیزری کانفوکالGrain softness protein - پروتئین نرمی دانهPIN - پین
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Tryptophanins (TRPs) are low molecular weight, tryptophan-rich, basic proteins found in oat (Avena sativa L.) seeds. Like their counterpart puroindolines (PINs) from wheat (Triticum aestivum L.), TRPs are thought to be involved in flour softness as well as disease resistance against phytopathogenic fungi. PINs are known to be the major components of 'friabilin' associated with the surface of water washed starch grains and possess lipid binding properties. Two polyclonal antisera against puroindoline-a (PIN-a), and puroindoline-b (PIN-b) respectively; and a monoclonal antiserum raised against 'friabilin' were used as primary antibodies in immunoblotting experiments. All antisera detected immunoreactive polypeptides, with approximate relative masses of 15-16Â kDa, in oat, wheat, and barley (Hordeum vulgare L.) seed extracts but not in rice (Oryza sativa L.), maize (Zea mays L.), bean (Phaseolus vulgaris L.), pea (Pisum sativum L.) and lentil (Lens culinaris Medic.) seed extracts. Immunoreactive polypeptides were detected in aqueous ethanol [52% (v/v) ethanol] seed extracts. Both anti-'friabilin' monoclonal and anti-PIN-b polyclonal antisera recognized 15 as well as 16Â kDa tryptophanins in oat seeds from different cultivars. On the other hand, anti-PIN-a polyclonal antiserum strongly cross-reacted with 16Â kDa TRP and weakly with 15Â kDa TRP. Tryptophanins were found to be associated with the surface of starch grains in oat endosperm tissue using both fluorescence and confocal laser scanning microscopies with anti-'friabilin' monoclonal antiserum. SDS-PAGE and immunoblotting assays revealed a gradual synthesis of TRPs as early as milk stage in developing oat seeds. On the other hand, TRPs tend to undergo degradation during seed germination.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Plant Science - Volume 172, Issue 3, March 2007, Pages 579-587
Journal: Plant Science - Volume 172, Issue 3, March 2007, Pages 579-587
نویسندگان
M. Mohammadi, M. Abbas Zaidi, A. Ochalski, M. Tanchak, I. Altosaar,