کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2053400 | 1074276 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Development of highly stable galectins: Truncation of the linker peptide confers protease-resistance on tandem-repeat type galectins
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Galectin-9 and galectin-8, members of β-galactoside-binding animal lectin family, are promising agents for the treatment of immune-related and neoplastic diseases. The proteins consist of two carbohydrate recognition domains joined by a linker peptide, which is highly susceptible to proteolysis. To increase protease resistance, we prepared mutant proteins by serial truncation of the linker peptide. As a result, mutant forms lacking the entire linker peptide were found to be highly stable against proteolysis and retained their biological activities. These mutant proteins might be useful tools for analyzing the biological functions and evaluating the therapeutic potential of galectin-9 and galectin-8.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 579, Issue 10, 11 April 2005, Pages 2058–2064
Journal: FEBS Letters - Volume 579, Issue 10, 11 April 2005, Pages 2058–2064
نویسندگان
Nozomu Nishi, Aiko Itoh, Aimi Fujiyama, Naoko Yoshida, Shin-ichi Araya, Mitsuomi Hirashima, Hiroki Shoji, Takanori Nakamura,