کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9886121 | 1537496 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
New GlcNAc/GalNAc-specific lectin from the ascidian Didemnum ternatanum
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کلمات کلیدی
PBSPAATBSHRPBSMPolyacrylamide - پلی آکریل آمیدBSA - BSAbovine serum albumin - آلبومین سرم گاوEDTA - اتیلن دی آمین تترا استیک اسید ethylenediamine tetraacetate - اتیلندیامین تتراسناتInvertebrate - بی مهرهTris-buffered saline - تریس بافر شورPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریHorseradish peroxidase - پراکسیداز هوررادیشSulfated polysaccharide - پلی ساکارید سولفاتGlycoprotein - گلیکوپروتئین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Previously we isolated GlcNAc-specific lectin (DTL) from the ascidian Didemnum ternatanum by affinity chromatography on cross-linked ovalbumin. Here we report the purification and characterization of new D-GlcNAc/D-GalNAc-specific lectin DTL-A from the same ascidian. This lectin was isolated from non-bound cross-linked ovalbumin fraction and further was purified by gel filtration on Sepharose CL-4B, affinity chromatography on GlcNAc-agarose and gel filtration on Superdex 200. SDS-polyacrylamide gel electrophoresis and gel filtration of purified lectin on Sepharose CL-4B indicates that it exists as large aggregates in the native state. Investigations of the carbohydrate specificity of DTL-A by enzyme-linked lectin assay suggest the multi-specificity of this lectin. DTL-A binds BSM, asialo-BSM as well as heparin and dextran sulfate. The binding of DTL-A to BSM was inhibited by monosaccharides D-GlcNAc and D-GalNAc, their α- but not β-anomers. Among polysaccharides and glycoconjugates, DTL-A binding to BSM was effectively inhibited by BSM, asialo-BSM, pronase-treated BSM and synthetic α-D-GalNAc-PAA. Fetuin and asialofetuin showed a much lower inhibitory potency, heparin and dextran sulfate were noninhibitory. On the other hand, DTL-A binding to heparin was effectively inhibited by dextran sulfate, fucoidan, whereas BSM showed insignificantly inhibitory effect. DTL-A binding to heparin was not inhibited by D-GlcNAc and D-GalNAc.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1723, Issues 1â3, 25 May 2005, Pages 82-90
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1723, Issues 1â3, 25 May 2005, Pages 82-90
نویسندگان
Valentina Molchanova, Irina Chikalovets, Wei Li, Stanislav Kobelev, Svetlana Kozyrevskaya, Raisa Bogdanovich, Eric Howard, Natalia Belogortseva,