Purification and Characterization of NAD-Specific 6-Phosphogluconate Dehydrogenase from Leuconostoc lactis SHO-54(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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概要

• 論文の詳細を見る

• The 6-phosphogluconate dehydrogenase (EC 1.1.1.44) from Leuconostoc lactis SHO-54 was purified with an overall yield of 38% and a specific activity of 140.0 units/mg protein. The enzyme had a tetrameric structure and a molecular mass of 32.8 kDa. The amino acid composition of the purified enzyme was determined, and the enzyme contained no sulfhydryl amino acids. The K_m values for 6-phosphogluconate and NAD were 0.95 mM and 0.32 mM, respectively.

• 社団法人日本生物工学会の論文
• 2004-08-25

著者

• Ohara Hitomi

  Toyota Biotechnology And Afforestation Laboratory

• Kondo Hitoshi

  Medical Development Department Medical Products Division Unitika Ltd.

• Kondo H

  Medical Development Department Medical Products Division Unitika Ltd.

• Uchida Kazuyuki

  Medical Development Department Medical Products Division Unitika Ltd.

• RUSSELL ROY

  Medical Development Department Medical Products Division, Unitika Ltd.

• Russell Roy

  Medical Development Department Medical Products Division Unitika Ltd.

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• Purification and Characterization of NAD-Specific 6-Phosphogluconate Dehydrogenase from Leuconostoc lactis SHO-54(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
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