Structural Properties of Recombinant Ovalbumin and Its Transformation into a Thermostabilized Form by Alkaline Treatment

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概要

• 論文の詳細を見る

• The recombinant ovalbumin produced in Escherichia coli was purified from the cytoplasmic fraction and analyzed for its chemical and conformational properties. The recombinant ovalbumin displayed almost exactly the same circular dichroism and intrinsic trytophan fluorescence spectra as egg white ovalbumin. As in the egg white protein, four cysteine sulfhydryls and one cystine disulfide were contained in the recombinant protein, according to the results of amino acid analyses; the disulfide bond was found by a peptide mapping analysis to correspond to the native cystine, Cys^<73>-Cys^<120>. According to a gel electrophoresis analysis, the presence of the disulfide bond was accounted for by specific oxidation of the corresponding cysteine residues during purification of the cytoplasmic protein. Unlike the identity in the conformational and peptide structures, none of the post-translational modifications (N-terminal acetylation, phosphorylation, and glycosylation) that are known with egg white ovalbumin were detected in the recombinant protein. The recombinant ovalbumin was transformed into a thermostabilized form in a similar manner to the transformation of egg white protein into S-oval-bumin; alkaline treatment increased the temperature for thermostability by 8.7℃. These data strongly suggest that the post-translational modifications of ovalbumin are not related to the formation mechanism for S-ovalbumin.

• 社団法人日本農芸化学会の論文
• 1999-08-23

著者

• Hirose M

  The Division Of Applied Life Sciences The Graduate School Of Agriculture Kyoto University

• Hirose Masaaki

  Graduate School Of Agriculture Kyoto Univ.

• Hirose Masaaki

  The Research Institute For Food Science Kyoto Univesity

• Hirose Masaaki

  Division Of Applied Life Sciences The Graduate School Of Agriculture Kyoto University

• Takahashi N

  Univ. Tokyo Tokyo Jpn

• TATSUMI Eizo

  The Research Institute for Food Science, Kyoto University

• TAKAHASHI Nobuyuki

  The Research Institute for Food Science, Kyoto University

• ARII Yasuhiro

  The Research Institute for Food Science, Kyoto Unviersity

• Takahashi Nobtaka

  Department Of Agricultural Chemistry The University Of Tokyo:(presnet Addresses) The Institute Of Ph

• Takahashi Nobutaka

  Frontier Research Program The Institute Of Physical And Chemical Research (rlken)

• Hirose Masaaki

  The Research Institute For Food Science Kyoto University

• Tsuji Naoki

  Department Of Clinical Laboratory Medicine Sapporo Medical University School Of Medicine

• Tatsumi E

  Kyoto Univ. Kyoto Jpn

• Tatsumi Eizo

  The Research Institute For Food Science Kyoto University

• Takeda Noboru

  Faculty Of Pharmaceutical Sciences Josai University

• Arii Yasuhiro

  Division Of Applied Life Sciences Graduate School Of Agriculture Kyoto University:(present Address)s

• Takahashi N

  Graduate School Of Agriculture Kyoto Univ.

• Takahashi Nobuyuki

  The Research Institute For Food Science Kyoto University

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