大鼠肝脏质膜中一种钙离子依赖性三磷酸腺苷焦磷酸水解酶。证明三磷酸腺苷类似物5'-[βγ-亚氨基]三磷酸腺苷和5'-[βγ-亚甲基]三磷酸腺苷是该酶的底物。
A calcium ion-dependent adenosine triphosphate pyrophosphohydrolase in plasma membrane from rat liver. Demonstration that the adenosine triphosphate analogues adenosine 5'-[betagamma-imido]triphosphate and adenosine 5'-[betagamma-methylene]-triphosphate are substrates for the enzyme.
作者信息
Flodgaard H, Torp-Pedersen C
出版信息
Biochem J. 1978 Jun 1;171(3):817-20. doi: 10.1042/bj1710817.
Abstract
An ATP pyrophosphohydrolase in a rat liver plasma-membrane subfraction was studied with respect to specific Ca2+ activation of the beta-phosphate bond hydrolysis. ATP and, in addition, adenosine 5'-[betagamma-imido]triphosphate and adenosine 5'-[betagamma-methlylene]triphosphate were substrates for Ca2+-stimulated enzymic hydrolysis of the beta-phosphate bond. A 15-fold activation was observed by raising the free Ca2+ concentration from 10(-7) to 10(-5) M. Mg2+ had little effect. Solubilization in 1% deoxycholate and partial purification on a sucrose density gradient resulted in a 5-fold increase in specific activity with unaltered Ca2+-stimulation pattern. The possible importance of the enzyme in Ca2+ transport is discussed.
摘要
针对大鼠肝细胞膜亚组分中的一种ATP焦磷酸水解酶，研究了其对β - 磷酸键水解的特异性Ca²⁺激活作用。ATP，此外还有腺苷5'-[βγ-亚氨基]三磷酸和腺苷5'-[βγ-亚甲基]三磷酸，都是Ca²⁺刺激的β - 磷酸键酶促水解的底物。通过将游离Ca²⁺浓度从10⁻⁷ M提高到10⁻⁵ M，观察到了15倍的激活作用。Mg²⁺的影响很小。用1%脱氧胆酸盐增溶并在蔗糖密度梯度上进行部分纯化，导致比活性提高了5倍，而Ca²⁺刺激模式未改变。讨论了该酶在Ca²⁺转运中的可能重要性。
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A calcium ion-dependent adenosine triphosphate pyrophosphohydrolase in plasma membrane from rat liver. Demonstration that the adenosine triphosphate analogues adenosine 5'-[betagamma-imido]triphosphate and adenosine 5'-[betagamma-methylene]-triphosphate are substrates for the enzyme.大鼠肝脏质膜中一种钙离子依赖性三磷酸腺苷焦磷酸水解酶。证明三磷酸腺苷类似物5'-[βγ-亚氨基]三磷酸腺苷和5'-[βγ-亚甲基]三磷酸腺苷是该酶的底物。
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