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[肌浆网Ca-ATP酶膜结合单体形式的Ca2+转运]

[Ca2+ transport by the membrane-bound monomeric form of Ca-ATPase of sarcoplasmic reticulum].

作者信息

Ritov V B, Shcherbakova N S

出版信息

Biull Eksp Biol Med. 1982 Apr;93(4):21-3.

PMID:6211201
Abstract

Chromatography of a mixture of phospholipid and Ca-dependent ATPase of sarcoplasmic reticulum solubilized with choleate in a column with anionite results in proteolyposome formation. It was shown that dilution of ATPase with phospholipids makes it possible to reduce the concentration of ATPase in the membrane. Using the bifunctional reagent difluorodinitrobenzene it was demonstrated that reduction of the ATPase concentration in the membrane leads to the dissociation of the enzyme to monomers. It was disclosed that the monomeric form of ATPase is capable of active Ca2+ transport.

摘要

用胆酸盐溶解的肌浆网磷脂和钙依赖性ATP酶混合物在阴离子交换柱上进行色谱分离会导致蛋白水解体的形成。结果表明,用磷脂稀释ATP酶能够降低膜中ATP酶的浓度。使用双功能试剂二氟二硝基苯表明,膜中ATP酶浓度的降低会导致酶解离为单体。据披露,ATP酶的单体形式能够进行活性Ca2+转运。

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