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A novel dinitrophenylglutathione‐stimulated ATPase is present in human erythrocyte membranes
Author(s) -
LaBelle Edward F.,
Singh Shivendra V.,
Ahmad Hassan,
Wronski Leszek,
Srivastava Satish K.,
Awasthi Yogesh C.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80583-0
Subject(s) - membrane , atpase , erythrocyte membrane , chemistry , biophysics , biochemistry , microbiology and biotechnology , enzyme , biology
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 Me 2+ 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.