Partial purification and characterization of the human erythrocyte Mg2+ ‐ATPase A candidate aminophospholipid translocase

FEBS Letters

Zachowski, Alain¹  Devaux, Philippe F.¹  Morrot, Gil¹ 

[1] Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France

关键词: Mg-ATPase;    Aminophospholipid translocase;    Phosphatidylserine;    Erythrocyte;    PS;    phosphatidylserine;    PE;    phosphatidylethanolamine;    PC;    phosphatidylcholine;    PA;    phosphatidic acid;    DPG;    diphosphatidylglycerol;    C12E9;    polyoxyethylene 9 lauryl ether;    EGTA;    ethyleneglycol bis(β-aminoethylether)-N;    N;    N′;    N′-tetraacetic acid;    DTE;    di-thio erythritol;    EDTA;    ethylene diamine tetraacetic acid;   

DOI  :  10.1016/0014-5793(90)81498-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A Mg²⁺-ATPase-enriched fraction was obtained from solubilized human erythrocyte membranes by ammonium sulphate precipitation and anion-exchange chromatography. The solubilized enzyme, of apparent molecular weight 120 kDa, requires phosphatidylserine to be fully active. Phosphatidylethanolamine but not other anionic phospholipids can only partially restore the activity. The Mg-ATPase has a low affinity for Mg²⁺-ATP and is inhibited by fluoride, vanadate, vanadyl and calcium ions. From these characteristics, we infer that this Mg²⁺-ATPase is the same protein as the aminophospholipid translocase which regulates the membrane phospholipid transverse distribution in human erythrocytes by actively transporting aminophospholipids from the outer to the inner monolayer.

【 授权许可】

Unknown