کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8328684 | 1540207 | 2018 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A novel core 1 O-linked glycan-specific binding lectin from the fruiting body of Hericium erinaceus
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
Thomsen-FriedenreichPMSFBSMPSMMOAGalNAcNeu5AcNeu5GcPNAN-acetylgalactosamineGlcNAcFucoseFucGbpspeanut agglutinin - آگلوتینین بادام زمینیN-acetylneuraminic acid - اسید N-استیلون اورامینیکN-glycolylneuraminic acid - اسید N-گلیکولیل نورامنیکcolumn volume - ستون حجمHEA - سرMass spectrometry - طیف سنجی جرمیphenylmethylsulfonyl fluoride - فنیل متیل سولفونیل فلورایدMushroom - قارچ یا ماشرومLectin - لکتینMatrix assisted laser desorption ionization-time of flight mass spectrometry - ماتریکس به زمان یونیزاسیون لیزر جذب طیف سنجی جرمی کمک کردMALDI-TOF MS - مالدی توف MSBovine submaxillary mucin - موکین submaxillary گاوN-acetylglucosamine - نیتستیگلوکوزامینHericium erinaceus - هریسیوم erinaceusCarbohydrate-binding proteins - پروتئین های اتصال دهنده کربوهیدراتHEL - کاملGal - گالGalactose - گالاکتوزمی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Mucin-type O-glycans are involved in biological functions on the cell surface as well as the glycoproteins and can also be used as specific carbohydrate biomarkers of many diseases. In this study, I purified a novel core 1 O-linked glycan specific lectin, Hericium erinaceus lecin (HeL), from the fruiting body of the mushroom Hericium erinaceus, which is known as the natural source for a sialic acid-binding lectin. Upon optimization of the purification conditions, a sequence of ion exchange, affinity, ion exchange, and size-exclusion chromatography resulted in the highest yield and best quality of lectin without protease activity. The resulting purified HeL is an apparent hexameric protein with a subunit molecular weight of 15 kDa, and a pI of 4.3. In hemagglutination inhibition assay, the purified lectin was only inhibited by glycoproteins containing mucin-type O-glycans and reacted weakly with Galβ(1,3)GalNAc. Glycan array analyses showed that HeL specifically interacts with core 1 O-linked glycans as well as extended O-glycan structures containing sialylation or fucosylation. The glycan binding specificity of HeL is comparable to that of peanut agglutinin for detection of a broader range of extended core 1 O-glycan structures. Taken together, these results provide an efficient and optimized procedure for the purification of HeL from the fruiting body of the mushroom Hericium erinaceus. Moreover, HeL represents a powerful tool for analyzing core 1 and extended core 1 O- glycan structures in diagnosis assays.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 107, Part B, February 2018, Pages 1528-1537
Journal: International Journal of Biological Macromolecules - Volume 107, Part B, February 2018, Pages 1528-1537
نویسندگان
Seonghun Kim,