Purification and Characterization of UDP-Arabinopyranose Mutase from Chlamydomonas reinhardtii
スポンサーリンク
概要
- 論文の詳細を見る
Chlamydomonas reinhardtii cells are surrounded by a mixture of hydroxyprolin-rich glycoproteins consisting of L-arabinose, D-galactose, D-glucose, and D-mannose residues. The L-arabinose residue is thought to be attached by a transfer of UDP-L-arabinofuranose (UDP-Araf), which is produced from UDP-L-arabinopyranose (UDP-Arap) by UDP-arabinopyranose mutase (UAM). UAM was purified from the cytosol to determine the involvement of C. reinhardtii UAM (CrUAM) in glycoprotein synthesis. CrUAM was purified 94-fold to electrophoretic homogeneity by hydrophobic and size-exclusion chromatography. CrUAM catalyzed the reversible conversion between UDP-Arap and UDP-Araf and exhibited autoglycosylation activity when UDP-D-[14C]glucose was added as substrate. Compared to the properties of native and recombinant CrUAM overexpressed in Escherichia coli, native CrUAM showed a higher affinity for UDP-Arap than recombinant CrUAM did. This increased affinity for UDP-Arap might have been caused by post-translational modifications that occur in eukaryotes but not in prokaryotes.
著者
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Konishi Teruko
Faculty Of Agriculture University Of The Ryukyus
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Yamashita Tetsuro
Faculty Of Agriculture Iwate University
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Ishii Tadashi
Forest And Forest Products Research Institute
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TAKEDA Takumi
Iwate Biotechnology Research Center
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SHIMOJIMA Mie
Tokyo Institute of Technology, Center for Biological Resources and Informatics
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KOTANI Ayana
Faculty of Agriculture, University of the Ryukyus
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TSUJI Maki
Faculty of Agriculture, University of the Ryukyus
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AZAMA Yasushi
Faculty of Agriculture, University of the Ryukyus
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