A novel dinitrophenylglutathione‐stimulated ATPase is present in human erythrocyte membranes

FEBS Letters

LaBelle, Edward F.¹  Singh, Shivendra V.¹  Ahmad, Hassan¹  Awasthi, Yogesh C.¹  Srivastava, Satish K.¹  Wronski, Leszek¹ 

[1] Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, TX 77550, USA

关键词: Erythrocyte;    Membrane;    Dinitrophenylglutathione;    Transport;   

DOI  :  10.1016/0014-5793(88)80583-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Vesicles prepared from human erythrocyte membranes were found to catalyze ATP hydrolysis that was stimulated by dinitrophenylglutathione (Dnp-SG). This activity was dependent on temperature and Me²⁺ and independent of ion pump ATPases present in erythrocyte membranes. The activity was a linear function of protein and time up to 60 min. The K _m values of ATPase for Dnp-SG and ATP were found to be 49 μM and 1.67 mM, respectively. This suggests that in erythrocytes, the transport of Dnp-SG requires direct enzymatic hydrolysis of ATP and both Dnp-SG-stimulated ATPase activity and the ATP-dependent efflux of Dnp-SG from erythrocytes represent different activities of the same protein.

【 授权许可】

Unknown