Calcium-dependent Properties of Peptidylarginine Deiminase from Rabbit Skeletal Muscle(Biological Chemistry)
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概要
- 論文の詳細を見る
Peptidylarginine deiminase, which catalyzes the deimination of arginyl residues in protein, required Ca^<2+> as an essential cofactor and the half-maximal activity was attained at 40〜60 μM Ca^<2+>. Other divalent cations were practically inactive except for Sr^<2+>, which was about 50% as active as Ca^<2+> when tested at 10mM. However, Sr^<2+> at less than the concentration of 100 μM had little or no activity. The direct Ca^<2+>-binding for the enzyme showed a sigmoidal curve with a transition midpoint of about 110 μM, indicating that the binding is cooperative. Analysis of Hill plots of the data revealed that the enzyme binds 3 mol of Ca^<2+>/mol of protein with an apparent dissociation constant of 110 μM. A conformational change upon Ca^<2+>-binding was also described for the enzyme using UV-difference spectra. The alteration could be attributed to an increased exposure of the aromatic residues to a more aqueous environment, as has been described for Ca^<2+>-binding proteins such as calmodulin. Phosphatidylserine enhanced the reaction velocity and concomitantly reduced the Ca^<2+>-requirement for the enzyme. These effects were stimulated by the addition of diacylglycerol. Diacylglycerol alone had little or no effect. On the other hand, calmodulin had no effect on the enzymatic activity over a wide range of Ca^<2+> concentrations. These suggest that the activity and Ca^<2+>-sensitivity of peptidylarginine deiminase is increased at the cell membrane.
- 社団法人日本農芸化学会の論文
- 1986-11-23
著者
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Sugawara Kiyoshi
Laboratories of Biochemistry, lbaraki University
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Takahara Hidenari
Laboratories of Biochemistry, lbaraki University
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Sugawara K
Ibaraki Univ. Ibaraki Jpn
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Takahara H
Ibaraki Univ. School Of Agriculture Ibaraki Jpn
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OKAMOTO Hiroomi
Laboratory of Biochemistry, Department of Agricultural Chemistry, Ibaraki University
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Okamoto Hiroomi
Laboratory Of Biochemistry Department Of Agricultural Chemistry Ibaraki University
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