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

Edward F. LaBelle; Shivendra V. Singh; Hassan Ahmad; Leszek Wronski; Satish K. Srivastava; Yogesh C. Awasthi

doi:10.1016/0014-5793(88)80583-0

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

Edward F. LaBelle, Shivendra V. Singh, Hassan Ahmad, Leszek Wronski, Satish K. Srivastava, Yogesh C. Awasthi

Research output: Contribution to journal › Article › peer-review

46 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	53-56
Number of pages	4
Journal	FEBS Letters
Volume	228
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(88)80583-0
State	Published - Feb 8 1988
Externally published	Yes

Keywords

Dinitrophenylglutathione
Erythrocyte
Membrane
Transport

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(88)80583-0

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title = "A novel dinitrophenylglutathione-stimulated ATPase is present in human erythrocyte membranes",

abstract = "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 Km 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.",

keywords = "Dinitrophenylglutathione, Erythrocyte, Membrane, Transport",

author = "LaBelle, {Edward F.} and Singh, {Shivendra V.} and Hassan Ahmad and Leszek Wronski and Srivastava, {Satish K.} and Awasthi, {Yogesh C.}",

note = "Funding Information: Acknowledgements: This investigation was supported in part by US PHS grant GM 32304, awarded by The National Institute of GeneralM edical Sciences, grants EY 04396 and EY 01677, awarded by The National Eye Institute, and grant CA 27967, awarded by The National Cancer Institute.",

year = "1988",

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doi = "10.1016/0014-5793(88)80583-0",

language = "English (US)",

volume = "228",

pages = "53--56",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

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TY - JOUR

T1 - A novel dinitrophenylglutathione-stimulated ATPase is present in human erythrocyte membranes

AU - LaBelle, Edward F.

AU - Singh, Shivendra V.

AU - Ahmad, Hassan

AU - Wronski, Leszek

AU - Srivastava, Satish K.

AU - Awasthi, Yogesh C.

N1 - Funding Information: Acknowledgements: This investigation was supported in part by US PHS grant GM 32304, awarded by The National Institute of GeneralM edical Sciences, grants EY 04396 and EY 01677, awarded by The National Eye Institute, and grant CA 27967, awarded by The National Cancer Institute.

PY - 1988/2/8

Y1 - 1988/2/8

N2 - 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 Km 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.

AB - 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 Km 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.

KW - Dinitrophenylglutathione

KW - Erythrocyte

KW - Membrane

KW - Transport

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SP - 53

EP - 56

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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