In Vivo Biotinylation of Fusion Proteins Expressed in Escherichia coli with a Sequence of Propionibacterium freudenreichii Transcarboxylase 1.3S Biotin Subunit

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概要

• 論文の詳細を見る

• Biotinylation of fusion proteins in E.coli was studied using a sequence of Propionibacterium freudenreichii transcarboxylase 1.3S biotin subunit. As the biotinylation sequence, we examined two sequences : one was of amino acid residues [84-123] of 1.3S, a partial sequence containing a region from a conserved tetrapeptide (Ala-Met-Bct-Met) around the biotinyl lysine(Bct) to the carboxyl terminal ; the other was of an almost entire sequence [18-123]. We constructed recombinant plasmids for fusion proteins of β-galactosidase, of chloramphenicol acetyltransferase, and of alkaline phosphatase. We found the biotinylation in the [18-123] sequence fused to alkaline phosphatase.

• 社団法人日本農芸化学会の論文
• 1992-07-23

著者

• YAMASAKI Makari

  Department of Agricultural Chemistry, the University of Tokyo

• YODA Koji

  Department of Biotechnology, University of Tokyo

• Yamano Naoko

  Government Industrial Research Institute

• Yoda Koji

  Department Of Agricultural Chemistry The University Of Tokyo

• Yamasaki Makari

  Department Of Agricultural Chemistry The University Of Tokyo

• KAWATA Yoshikazu

  Government Industrial Research Institute

• KOJIMA Hiroyuki

  Government Industrial Research Institute

• Kawata Yoshikazu

  Special Division For Green Life Technology National Institute Of Advanced Industrial Science And Tec

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