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成骨细胞质膜中(Ca2+ + Mg2+)-ATP酶系统的特性分析。

Characterization of a (Ca2+ + Mg2+)-ATPase system in the osteoblast plasma membrane.

作者信息

Shen V, Hruska K, Avioli L V

机构信息

Division of Bone and Mineral Disease, Washington University School of Medicine, St. Louis, MO.

出版信息

Bone. 1988;9(5):325-9. doi: 10.1016/8756-3282(88)90017-8.

Abstract

A high affinity, calmodulin-sensitive (Ca2 + Mg2+)-ATPase was demonstrated in the plasma membrane preparation of three different osteosarcoma cell lines previously demonstrated to respond to parathyroid hormone with an increase in cytosolic calcium and a decrease in pH. The maximal velocity of the enzyme activity in the membrane preparations ranged from 0.83 to 2.42 nmol Pi released per min per mg protein with half-saturation constants of 26 nM of free Ca. The enzyme activity was not affected by Na+, K+, ouabain and azide, and exhibited an absolute requirement for Mg2+ ions. These results suggest a possible role for a membrane Ca2 + Mg2+-ATPase in initiating and perpetuating the ionic control of osteoblastic function.

摘要

在三种不同骨肉瘤细胞系的质膜制剂中证实了一种高亲和力、钙调蛋白敏感的(Ca2 + Mg2 +)-ATP酶,先前已证明这三种细胞系对甲状旁腺激素有反应,即细胞溶质钙增加和pH值降低。膜制剂中酶活性的最大速度范围为每分钟每毫克蛋白质释放0.83至2.42 nmol无机磷,游离钙的半饱和常数为26 nM。酶活性不受Na +、K +、哇巴因和叠氮化物的影响,并且对Mg2 +离子有绝对需求。这些结果表明膜Ca2 + Mg2 +-ATP酶在启动和成骨细胞功能的离子控制过程中可能发挥作用。

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