کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1389085 | 982840 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Convenient enzymatic synthesis of a p-nitrophenyl oligosaccharide series of sialyl N-acetyllactosamine, sialyl Lex and relevant compounds
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Convenient enzymatic synthesis of a p-nitrophenyl oligosaccharide series of sialyl N-acetyllactosamine, sialyl Lex and relevant compounds Convenient enzymatic synthesis of a p-nitrophenyl oligosaccharide series of sialyl N-acetyllactosamine, sialyl Lex and relevant compounds](/preview/png/1389085.png)
چکیده انگلیسی
From the β-d-Gal-(1â4)-β-d-GlcNAc-OC6H4NO2-p (1) prepared by the transglycosylation of β-galactosidase from Bacillus circulans, α-d-Neu5Ac-(2â3)-β-d-Gal-(1â4)-β-d-GlcNAc-OC6H4NO2-p (9) and α-d-Neu5Ac-(2â6)-β-d-Gal-(1â4)-β-d-GlcNAc-OC6H4NO2-p (10) were effectively synthesized with an equimolar ratio of CMP-Neu5Ac by recombinant rat α-(2â3)-N-sialyltransferase and rat liver α-(2â6)-N-sialyltransferase, respectively. The former enzyme also transferred effectively the Neu5Ac residue from CMP-Neu5Ac to the location of OH-3 in the non-reducing terminal of β-d-Gal-(1â4)-β-d-Gal-OC6H4NO2-p or β-d-Gal-(1â4)-β-d-Gal-(1â4)-β-d-GlcNAc-OC6H4NO2-p, while the latter enzyme did not. In the case of equimolar ratio of GDP-Fuc/acceptor, 1 and 9 were further fucosylated quantitatively to form β-d-Gal-(1â4)-β-d-(α-l-Fuc-(1â3)-)-GlcNAc-OC6H4NO2-p (14) and α-d-Neu5Ac-(2â3)-β-d-Gal-(1â4)-β-d-(α-l-Fuc-(1â3)-)-GlcNAc-OC6H4NO2-p (13) by recombinant human α-(1â3)-fucosyltransferase VII, respectively.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Carbohydrate Research - Volume 340, Issue 16, 21 November 2005, Pages 2469-2475
Journal: Carbohydrate Research - Volume 340, Issue 16, 21 November 2005, Pages 2469-2475
نویسندگان
Xiaoxiong Zeng, Hirotaka Uzawa,