Reconstitution of Fragmentary Form of Thermostable Alanine Racemase
スポンサーリンク
概要
- 論文の詳細を見る
The fragmentary form of alanine racemase from Bacillus stearothermophilus is composed of two sets of two different polypeptides corresponding to the two domains of the subunit of wild-type enzyme. It was denatured with 6M guanidium hydrochloride to be separated into pieces, and renatured by dilution with about 50% recovery of the activity. The two kinds of polypeptides (i. e. , large and a small fragments) were isolated by gel filtration in the presence of 4M guanidium hydrochloride. The CD spectra obtained by summation of the spectra of the refolded fragments were closely similar to that of the native fragmentary enzyme. The lysine residue to which PLP is bound in the wild-type enzyme occurs in the large peptide of the fragmentary enzyme containing the amino terminus of the wild-type enzyme. The visible spectrum of the large peptide refolded, however, indicated that PLP was not bound to it. The large peptide alone had no significant activity, but it was activated by incubation with the small peptide. Accordingly, co-existence of both peptide fragments is necessary for folding of a complex of the two kinds of peptide to form an active structure.
- 社団法人日本農芸化学会の論文
- 1995-06-23
著者
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Esaki N
Institute For Chemical Research Kyoto University
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Esaki Nobuyoshi
Kyoto Univ.
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Esaki Nobuyoshi
Nstitute For Chemical Research Kyoto University
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Ezaki Nobuyoshi
Laboratory Of Microbial Biochemistry Institute For Chemical Research Kyoto University
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Esaki Nobuyoshi
Institute for Chemical Research, Kyoto University
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YOSHIMURA Tohru
Institute for Chemical Research, Kyoto University
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SODA Kenji
Institute for Chemical Research, Kyoto University
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Soda Kenji
Department Of Biotechnology Kansai University
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Soda Kenji
Laboratory Of Microbial Biochemistry Institute For Chemical Research Kyoto University
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Soda Kenji
Institute For Chemical Resarch Kyoto University
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Lim Young
Institute For Chemical Research Kyoto University
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Yoshimura Tohru
Institute For Chemical Research Kyoto University:(present Address)department Of Applied Molecular Bi
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Toyama Hirohide
Institute For Chemical Research Kyoto University
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Esaki Nobuyoshi
Kyoto Univ. Kyoto Jpn
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Esaki Nobuyoshi
Institute For Chemical Resarch Kyoto University
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LIM YOUNG-HEE
Institute for Chemical Research, Kyoto University
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Soda K
Department Of Biotechnology Kansai University
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