パン酵母オルニチン・アミノ基転移酵素の精製と性質

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書誌事項

タイトル別名
  • Purification and Properties of Yeast Ornithine Aminotransferase
  • パン コウボ オルニチン アミノキ テンイ コウソ ノ セイセイ ト セイシツ

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抄録

Ornithine aminotransferase (EC 2.6.1.13) was purified from baker's yeast (Saccharomyces cerevisiae) with following steps : aceton powder, crude extract, nucleic. acid digestion by ribonuclease T_1,protamine sulfate treatment, heat treatment, ammonium sulfate fractionation and DEAE-Sephadex column chromatography. Finally the specific activity increased 10-fold times and about 7% of the enzyme activity was recovered. The enzyme was unstable and showed the optimum pH at 7.0 to 7.5. Km values determined kinetically were as follows ; for ornithine, 1.2〜2.5×10^<-3>M and for α-ketoglutarate, 6.7×10^<-3>M. Branched chain amino acids were weakly inhibitory and K_i value for L-valine was 4.3×10^<-3>M. These properties were compared with those of rat liver enzyme.

収録刊行物

  • ビタミン

    ビタミン 51 (1), 7-10, 1977

    公益社団法人 日本ビタミン学会

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