魚類筋肉ミオキナーゼに関する研究-II 精製コイ筋肉ミオキナーゼの酵素化学的性質について

福島 正和; 林 征一; 大城 善太郎

doi:10.2331/suisan.40.299

魚類筋肉ミオキナーゼに関する研究-II

精製コイ筋肉ミオキナーゼの酵素化学的性質について

福島正和, 林征一, 大城善太郎

著者情報

ジャーナルフリー

1974 年 40 巻 3 号 p. 299-302

DOI https://doi.org/10.2331/suisan.40.299

詳細

発行日: 1974/03/25 受付日: - J-STAGE公開日: 2008/02/29 受理日: 1973/12/10 早期公開日: - 改訂日: -
訂正情報
訂正日: 2008/02/29 訂正理由: - 訂正箇所: 論文抄録訂正内容: Wrong : Previously, the authors reported on the purification of myokinase I and II from the carp muscle by ammonium sulfate fractionation, Sephadex gel filtration, and by DEAE-cellulose and CM-cellulose column chromatography.
In this paper, studies on some properties of these purified myokinase isozymes were reported.
The molecular weights of myokinase I and II, determined both by gel filtration on Sephadex G-75 and by electrophoresis on SDS-polyacrylamide gel, were 27, 000 and 22, 000, respectively.
Influences of pH and temperature on the transphosphorylysis of ADP by these two isozymes were almost similar, and enzymatic reactions were ascertained to be optimally active at pH 7.5 and temperature 36-38°C.
Carp myokinase isozymes were found to be specific for ADP, whereas they were ascertained not to transphosphorylyse the following sorts of nucleoside-5′-diphosphate: GDP, IDP, CDP and UDP. These results show the extremely high specificity of the carp myokinase isozymes.
Right : Previously, the authors reported on the purification of myokinase I and II from the carp muscle by ammonium sulfate fractionation, Sephadex gel filtration, and by DEAE-cellulose and CM-cellulose column chromatography.
In this paper, studies on some properties of these purified myokinase isozymes were reported.
The molecular weights of myokinase I and II, determined both by gel filtration on Sephadex G-75 and by electrophoresis on SDS-polyacrylamide gel, were 27, 000 and 22, 000, respectively.
Influences of pH and temperature on the transphosphorylysis of ADP by these two isozymes were almost similar, and enzymatic reactions were ascertained to be optimally active at pH 7.5 and temperature 36-38°C.
Carp myokinase isozymes were found to be specific for ADP, whereas they were ascertained not to transphosphorylyse the following sorts of nucleoside-5'-diphosphate: GDP, IDP, CDP and UDP. These results show the extremely high specificity of the carp myokinase isozymes.

訂正日: 2008/02/29 訂正理由: - 訂正箇所: PDFファイル訂正内容: -

抄録

Previously, the authors reported on the purification of myokinase I and II from the carp muscle by ammonium sulfate fractionation, Sephadex gel filtration, and by DEAE-cellulose and CM-cellulose column chromatography.
In this paper, studies on some properties of these purified myokinase isozymes were reported.
The molecular weights of myokinase I and II, determined both by gel filtration on Sephadex G-75 and by electrophoresis on SDS-polyacrylamide gel, were 27, 000 and 22, 000, respectively.
Influences of pH and temperature on the transphosphorylysis of ADP by these two isozymes were almost similar, and enzymatic reactions were ascertained to be optimally active at pH 7.5 and temperature 36-38°C.
Carp myokinase isozymes were found to be specific for ADP, whereas they were ascertained not to transphosphorylyse the following sorts of nucleoside-5'-diphosphate: GDP, IDP, CDP and UDP. These results show the extremely high specificity of the carp myokinase isozymes.

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