Proteolytic Release of Dehydrodolichyl Diphosphate Synthase from Pig Testis Microsomes

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概要

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• Pig testicular dehydrodolichyl diphosphate synthase was released in a soluble form out of microsomes by controlled proteolysis with trypsin or papain. Approximately 25% of the microsomal enzyme activity was recovered in the 115,000×g supernatant fraction when the microsomes were treated with trypsin at 4℃ for 1 h. Similar proteolytic release of microsomal enzyme was also observed with the treatment with papain. The K_m, optimal pH, Mg^<2+> dependency, and ion strength dependency of the enzyme released by trypsin were similar to those of the microsomal enzyme. The microsomal enzyme was active even in the absence of detergents, while the released enzyme required detergents for activity. Gel filtration of the released enzyme gave a peak of dehydrodolichyl diphosphate synthase activity, which appeared between 150-kDa and 50-kDa molecular mass markers.

• 社団法人日本農芸化学会の論文
• 1996-07-23

著者

• OGURA Kyozo

  Institute of Chemical Reaction Science, Tohoku University

• Ogura Kyozo

  Institute For Chemical Reaction Science Tohoku University

• SAGAMI Hiroshi

  Institute for Chemical Reaction Science, Tohoku University

• Sagami H

  Tohoku Univ. Sendai

• Sagami Hiroshi

  Institute Chemical Reaction Science Tohoku University

• KURISAKI Akira

  Institute for Chemical Reaction Science, Tohoku University

• Kurisaki Akira

  Institute For Chemical Reaction Science Tohoku University

関連論文

• Recognition of Allylic Substrates in Sulfolobus acidocaldarius Geranylgeranyl Diphosphate Synthase: Analysis Using Mutated Enzymes and Artificial Allylic Substrates^1
• An Artificial Substrate for the Thermostable Farnesyl Diphosphate Synthase from Bacillus stearothermophilus
• Farnesyl Diphosphate Synthase Reactions with Dimethylally Diphosphate Analogues Having Oxygen Atoms in Their Chains
• Farnesyl Diphosphate Synthase Reactions of Geranyl Diphosphate Analogues Having Oxygen Atoms in Their Alkyl Chains
• Subcellular Fractionation of Polyprenyl Diphosphate Synthase Activities Responsible for the Syntheses of Polyprenols and Dolichols in Spinach Leaves
• The Carboxyl-terminal Region of the Geranylgeranyl Diphosphate Synthase is Indispensable for the Stabilization of the Region Involved in Substrate Binding and Catalysis
• Human Geranylgeranyl Diphosphate Synthase is an Octamer in Solution
• Relationship between Intron 4b Splicing of the Rat Geranylgeranyl Diphosphate Synthase Gene and the Active Enzyme Expression Level
• Proteolytic Release of Dehydrodolichyl Diphosphate Synthase from Pig Testis Microsomes
• Neuronal cell type-specific promoter of the α CaM kinase II gene is activated by Zic2, a Zic family zinc finger protein
• Intersubunit Structure within Heterodimers of Medium-Chain Prenyl Diphosphate Synthases. Formation of a Hybrid-Type Heptaprenyl Diphosphate Synthase
• Study on the Biosynthesis of Dolichol in Yeast : Recognition of the Prenyl Chain Length in Polyprenol Reduction

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