کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7588021 | 1492082 | 2016 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Pin p 1 is a major allergen in pine nut and the first food allergen described in the plant group of gymnosperms
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کلمات کلیدی
TBSTabridged universal amplification primerAUAPadapter primerTMBPBSTHRPTBSPVDFBasophil activation test - آزمون فعال سازی بازوفیلAlbumin - آلبومینTree nut allergy - آلرژی مهره درختInternational Union of Immunological Societies - اتحادیه بین المللی انجمن های ایمنیIUIS - بار، IUI شدندtetramethylbenzidine - تترامتیل بنزیدینTris-buffered saline - تریس بافر شورRoom temperature - دمای اتاقpolyvinylidene difluoride - دی فلوئورید پلی وینیلیدینHorseradish peroxidase - پراکسیداز هوررادیشoptical density - چگالی نوری
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Pin p 1 is a major allergen in pine nut and the first food allergen described in the plant group of gymnosperms Pin p 1 is a major allergen in pine nut and the first food allergen described in the plant group of gymnosperms](/preview/png/7588021.png)
چکیده انگلیسی
This study aimed to report the complete sequence of a 2S albumin purified from pine nut and to analyze its allergenic properties. Individual recognition of this protein by serum IgE from pine nut-allergic patients was assessed. IgE cross-linking capacity was analyzed in a basophil activation test. Inhibition of IgE-binding and stability to heating was also assessed. The complete nucleotide sequence was obtained and a phylogenetic study was carried out. 2S albumin from pine nut (registered as Pin p 1.0101) was recognized by IgE of 75% of sera. The allergen was heat-stable and had a robust capacity to inhibit IgE-binding to whole pine nut extract. The IgE cross-linking capacity of Pin p 1 on basophils was also demonstrated. Despite the low homology of Pin p 1 sequence with other allergenic 2S albumins from angiosperms, Pin p 1 contains the typical skeleton of 8 cysteine residues, important for its α-helixes enriched structure.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 210, 1 November 2016, Pages 70-77
Journal: Food Chemistry - Volume 210, 1 November 2016, Pages 70-77
نویسندگان
Beatriz Cabanillas, Jesus F. Crespo, Soheila J. Maleki, Julia Rodriguez, Natalija Novak,