The Subunit Structure of Nitrite Reductase Purified from the Denitrifier Achromobacter cycloclastes

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概要

• 論文の詳細を見る

• The copper-contining nitrite reductase of Achromobacter cycloclastes has been considered to be a homotrimer with three identical subunits both in the crystal and in solution. In this study, however, the enzyme was found to be a heterotrimer consisting of two subunits with molecular masses of 37 kDa and 36.2 kDa, and the 37 kDa subunit was 6 amino acid residues longer than the smaller subunit. Signal-peptide cleavage sites in its N-terminal region are discussed.

• 社団法人日本農芸化学会の論文
• 1999-11-23

著者

• Inatomi Kenichi

  Advanced R & D Center, Mitsubishi Electric Corp.

• Inatomi Kenichi

  Advanced Technology R & D Center, Mitsubishi Electric Corp.

関連論文

• B22-036 AN ARTIFICIAL GEL STRUCTURE FABRICATED BY SILICON MICROMACHINING
• The Subunit Structure of Nitrite Reductase Purified from the Denitrifier Achromobacter cycloclastes

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