Comparison and Characterization of Arginine Kinases Purified from the Prawn Penaeus japonicus(Kurumaebi) and the Swimming Crab Portunus trituberculatus(Gazami)(Biological Chemistry)

スポンサーリンク

概要

• 論文の詳細を見る

• The physico-chemical characteristics of purified arginine kinases from prawn and swimming crab were examined. The molecular weights of prawn and swimming crab enzymes were 40,500 and 40,000, respectively. Amino acid analysis indicated that there were some differences in the contents of proline, glycine, methionine, and lysine. The other amino acid compositions of these enzymes resembled each other. Both enzymes were stable up to 20℃ when they were treated for 10min at various temperature levels. The enzymes lost their activities at temperatures higher than 25℃. They were more stable at pH 8.0 than pH 7.0. The optimum temperature for the enzyme of prawn was about 42℃ and that for swimming crab was about 40℃. The pH optima for the activity of arginine kinase of prawn in the forward and in the reverse reactions were found to be 9.0 and 6.1, respectively. For the swimming crab, the similar optimum pHs at 9.2 in the forward reaction and 5.8 in the reverse reaction were observed. Both enzymes were activated most strongly with Mg^<2+> and Mn^<2+> followed by Ca^<2+>, Co^<2+>, and Fe^<2+>. The enzymes were not activated by Sr^<2+>, Cu^<2+>, or Zn^<2+>. The optimum molar ratio of Mg^<2+> : ATP in the forward reaction of prawn and swimming crab was found to be 1 : 1, and the molar ratio of Mg^<2+> : ADP in the reverse reaction was 4 : 1 in both cases. Kinetic studies indicated that dissociation constants were rather different. In the prawn, dissociation constants for arginine, ATP, AP, and ADP were 0.19, 0.31, 0.67, and 0.29mM, respectively, but in the swimming crab, they were 0.10, 0.18, 0.22, and 0.11mM, respectively.

• 社団法人日本農芸化学会の論文
• 1989-09-23

著者

• Shimizu Chiaki

  Fisheries Research Laboratory Faculty Of Agriculture The University Of Tokyo

• Shimizu Chiaki

  Fisheries Laboratory Faculty Of Agriculture University Of Tokyo

• LIVERA W.

  Fisheries Laboratory, Faculty of Agriculture, The University of Tokyo

• Livera W.

  Fisheries Laboratory Faculty Of Agriculture The University Of Tokyo

関連論文

• Kinetics of a Chitinase from a Prawn, Penaeus japonicus(Biological Chemistry)
• Purifications and Some Properties of Chitinase from the Liver of a Prawn, Penaeus japonicus(Biological Chemistry)
• Purification and Some Properties of Chitinase from the Stomach of Japanese Eel, Anguilla japonica(Biological Chemistry)
• Fluorescence High Performance Liquid Chromatography of Eicosapentaenoic Acid in Serum and Vital Blood of Fishes and in Body Fluid of Plankton after Labeling with 9-Anthryldiazomethane (生体成分の高速液体クロマトグラフィ-)
• Comparison and Characterization of Arginine Kinases Purified from the Prawn Penaeus japonicus(Kurumaebi) and the Swimming Crab Portunus trituberculatus(Gazami)(Biological Chemistry)
• Seasonal changes in eicosapentaenoic and arachidonic acid contents in Bivalves and plankton collected from lake hamana.
• Seasonal movements of phosphorus and iron compounds, dissolved hydrogen sulfide, and others in anoxic seawater at lake hamana.

スポンサーリンク