マサバ血合肉中のイノシン酸分解酵素の分離・精製及びその諸性質

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タイトル別名
  • Purification and properties of acid phosphomonoesterase from the dark muscle of common mackerel.
  • マサバ チアイ ニクチュウ ノ イノシンサン ブンカイ コウソ ノ ブンリ セ

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抄録

It has been shown that the rapid degradation of inosinic acid (IMP) in the dark muscle of common mackerel Scomber japonicus is possibly catalized by an enzyme having high activity at pH 6.0. The enzyme was extracted from acetone powder and purified by the two steps of affinity chromatography on Concanavalin A-Sepharose and DEAE-cellulose chromatography. The purified enzyme was shown to be homogeneous by disc polyacrylamide gel electophoresis and its molecular weight was estimated to be about 9×104 by gel filtration. The enzyme was identified as acid phosphomonoesterase (EC 3.1.3.2), since it hydrolyzed 5'-IMP optimally at pH 5.5 and hydrolyzed various phosphorylated compounds including 5'-nucleotides, 3'-nucleo-tides, glucose-6-phosphate, β-glycerophosphate and p-nitrophenyl phosphate (p-NPP). The enzyme was inhibited by Cu2+, Zn2+, Fe2+ and NaF, but was not affected by Mg2+, Mn2+, Co2+, Ni2+, Ca2+, EDTA and iodoacetic acid. The presence of the other acid phosphatase which hydrolyzes p-NPP but not 5'-IMP was presumed in an unadsorbed fraction to Concanavalin A-Sepharose.

収録刊行物

  • 日本水産学会誌

    日本水産学会誌 54 (3), 463-468, 1988

    公益社団法人 日本水産学会

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