<i>In Vivo</i>Biotinylation of Fusion Proteins Expressed in<i>Escherichia coli</i>with a Sequence of<i>Propionibacterium freudenreichii</i>Transcarboxylase 1.3S Biotin Subunit
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- タイトル別名
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- In Vivo Biothinylation of Fusion Proteins Expressed in Escherichia coli with a Sequence of Propionibacterium freudenreichii Transcarboxylase 1.3S Biotin Subunit.
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説明
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.
収録刊行物
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- Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ
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Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ 56 (7), 1017-1026, 1992
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681447786880
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- NII論文ID
- 110002680677
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- PubMed
- 1368826
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- 本文言語コード
- en
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- journal article
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