کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10765944 | 1050618 | 2009 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Analysis of xylosyltransferase II binding to the anticoagulant heparin
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کلمات کلیدی
GAGXylosyltransferaseXylTamino acid - آمینو اسیدinclusion body - بدن درگیرHeparin - هپارین Proteoglycan - پروتئوگلیکانmaltose binding protein - پروتئین متصل به مالتوزHeparin affinity chromatography - کروماتوگرافی کربن هپارینGlutathion-S-Transferase - گلوتاتیون-س-ترانسفرازGlycosaminoglycan - گلیکوزآمینوگلیکان
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The key enzymes in the biosynthetic pathway of glycosaminoglycan production are represented by the human xylosyltransferase I and its isoform II (XylT-I and XylT-II). The glycosaminoglycan heparin interacts with a variety of proteins, thereby regulating their activities, also those of xylosyltransferases. The identification of unknown amino acids responsible for heparin-binding of XylT-II was addressed in this study. Thus, six XylT-II fragments were designed as fusion proteins with MBP and we received soluble and purified MBP/XylT-II from Escherichia coli. Heparin-binding studies showed that all fragments bound with low affinity to heparin. Prolonging of XylT-II fragments did not account for a cooperative effect of multiple heparin-binding motifs and in turn for a stronger heparin-binding. Sequence alignment and surface polarity plot led to the identification of two highly positively charged Cardin-Weintraub motifs with surface accessibility, resulting in combination with short clusters of basic amino acids for strong heparin-binding of native xylosyltransferases.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 383, Issue 1, 22 May 2009, Pages 4-10
Journal: Biochemical and Biophysical Research Communications - Volume 383, Issue 1, 22 May 2009, Pages 4-10
نویسندگان
Javier Carrera Casanova, Michael Ambrosius, Joachim Kuhn, Knut Kleesiek, Christian Götting,