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  1. 010 学術雑誌論文
  2. 桑島, 邦博 / KUWAJIMA, Kunihiro

Expression of a synthetic gene encoding canine milk lysozyme in Escherichia coli and characterization of the expressed protein

https://ir.soken.ac.jp/records/4289
https://ir.soken.ac.jp/records/4289
93ad5503-de40-42af-a780-7389a5be5693
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-03-12
タイトル
タイトル Expression of a synthetic gene encoding canine milk lysozyme in Escherichia coli and characterization of the expressed protein
タイトル
タイトル Expression of a synthetic gene encoding canine milk lysozyme in Escherichia coli and characterization of the expressed protein
言語 en
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 KOSHIBA, Takumi

× KOSHIBA, Takumi

KOSHIBA, Takumi

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KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

KUWAJIMA, Kunihiro

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et, al.

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et, al.

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著者別名 桑島, 邦博

× 桑島, 邦博

桑島, 邦博

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抄録
内容記述タイプ Abstract
内容記述 A high-expression plasmid of the canine milk lysozyme, which belongs to the family of calcium-binding lysozymes, was constructed in order to study its physico-chemical properties. Because the cDNA sequence of the protein has not yet been determined, a 400 base-pair gene encoding canine milk lysozyme was first designed on the basis of the known amino acid sequence. The gene was constructed by an enzymatic assembly of 21 chemically synthesized oligonucleotides and inserted into an Escherichia coli expression vector by stepwise ligation. The expression plasmid thus constructed was transformed into BL21(DE3)/pLysS cells. The gene product accumulated as inclusion bodies in an insoluble fraction. Recombinant canine milk lysozyme was obtained by purification and refolding of the product and showed the same characteristics in terms of bacteriolytic activity and far- and near-UV circular dichroism spectra as the authentic protein. The NMR spectra of refolded lysozyme were also characteristic of a native globular protein. It was concluded that recombinant canine milk lysozyme was folded into the correct native structure. Moreover, the thermal unfolding profiles of the refolded recombinant lysozyme showed a stable equilibrium intermediate, indicating that the molten globule state of this protein was extraordinarily stable. This expression system of canine milk lysozyme will enable biophysical and structural studies of this protein to be extended.
書誌情報 Protein Engineering, Design and Selection
en : Protein Engineering, Design and Selection

巻 12, 号 5, p. 429-435, 発行日 1999
出版者
出版者 Oxford University Press
ISSN
収録物識別子タイプ ISSN
収録物識別子 1741-0126
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1093/protein/12.5.429
関連名称 10.1093/protein/12.5.429
権利
権利情報 © Oxford University Press
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