Enhancement of Thermostability of Firefly Luciferase from Luciola lateralis by a Single Amino Acid Substitution
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概要
- 論文の詳細を見る
We constructed firedly luciferase mutants from Luciola lateralis in which Ala at position 217 was replaced by each of three hydrophobic amino acid residues (Ile, Leu, and Val). These mutants were superior to the wild-type in thermostability. Especially, the purified Ala217Leu mutant still maintained over 70% of the initial activity after 60min at 50℃. This mutant is the most thermostable firefly luciferase obtained.
- 社団法人日本農芸化学会の論文
- 1994-06-23
著者
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Kajiyama Noboru
Department Of Applied Biochemistry Faculty Of Applied Biological Sciences Hiroshima University
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Nakano Eiichi
Research And Development Division Kikkoman Corporation
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Kajiyama N
Kikkoman Corp. Chiba Jpn
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Kajiyama Naoki
Research And Development Division Kikkoman Corporation
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