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Study on the Tripolyphosphatase (TPPase) Property of Bighead Carp (Aristichthys nobilis) Myosin Subfragment-1 被引量:1

Study on the Tripolyphosphatase (TPPase) Property of Bighead Carp (Aristichthys nobilis) Myosin Subfragment-1
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摘要 Myosin subfragment-1 was prepared from the myofibrils of bighead carp (Aristichthys nobilis). The myosin subfrag- ment-1 was proved to have the activity of tripolyphosphatase (TPPase) responding to the hydrolysis of sodium tripolyphosphate (STPP). The optimum temperature and pH for the TPPase of myosin subfragment-1 were 30℃ and pH 5.0, and at pH 8.0 the TPPase also showed a high activity. Mg2+ was necessary to TPPase. The TPPase activity of myosin subfragment-1 was activated by Mg2+ under low concentrations, but was inhibited when the concentration was over 17 mmolL-1. The TPPase activity was also affected by KCl. The optimum concentration of KCl for TPPase was 0.3 molL-1 under the condition of 17 mmolL-1 Mg2+. The TPPase activity was significantly inhibited by EDTA-Na2. Reagents such as KBr, KI and KIO3 could inhibit the TPPase effectively. K2Cr2O7 as well as KMnO7 and KNO3 exhibited weak inhibiting effects. The TPPase converted STPP to pyrophosphate (PP) and orthophosphate (Pi) stoichiometrically with a KM of 3.2 mmolL-1. Myosin subfragment-1 was prepared from the myofibrils of bighead carp (Aristichthys nobilis). The myosin subfragment-1 was proved to have the activity of tripolyphosphatase (TPPase) responding to the hydrolysis of sodium tripolyphosphate (STPP). The optimum temperature and pH for the TPPase of myosin subfragment-1 were 30℃ and pH 5.0, and at pH 8.0 the TPPase also showed a high activity. Mg^2+ was necessary to TPPase. The TPPase activity of myosin subfragment-1 was activated by Mg^2+ under low concentrations, but was inhibited when the concentration was over 17 mmolL^-1. The TPPase activity was also affected by KCl. The optimum concentration of KCl for TPPase was 0.3 molL^-1 under the condition of 17 mmolL^-1 Mg^2+. The TPPase activity was significantly inhibited by EDTA-Na2. Reagents such as KBr, KI and KIO3 could inhibit the TPPase effectively. K2Cr2O7 as well as KMnO7 and KNO3 exhibited weak inhibiting effects. The TPPase converted STPP to pyrophosphate (PP) and orthophosphate (Pi) stoichiometrically with a KM of 3.2 mmolL^-1.
出处 《Journal of Ocean University of China》 SCIE CAS 2007年第4期398-402,共5页 中国海洋大学学报(英文版)
基金 This work was supported by the National Natural Science Foundation of China (No. 30671632) supported by the National High-tech Research and Development Project of China (No. 2006AA09Z444).
关键词 myosin subfragment-1 tripolyphosphatase (TPPase) bighead carp Aristichthys nobilis 肌浆球蛋白亚碎片-1 生物特性 花鲢 胖头鱼 海洋生物
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参考文献12

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同被引文献17

  • 1彭增起,周光宏,徐幸莲,吴菊清.四种多聚磷酸钠在鸡胸肉中水解的^(31)P核磁共振研究[J].食品科学,2005,26(8):61-65. 被引量:10
  • 2高瑞昌,薛长湖,李兆杰,薛勇,董平.鳙肌原纤维三聚磷酸盐水解酶(TPPase)的活性[J].水产学报,2006,30(5):695-700. 被引量:5
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