Abstract
A highly purified plasma membrane fraction isolated from rat hepatocytes was found to catalyze the hydrolysis of ATP in response to micromolar concentrations of glutathione disulfide (GSSG). This process exhibited distinct kinetic parameters suggesting the existence of both a high and low affinity component. The apparent K(m) values (GSSG) for ATP hydrolysis were 140 μM and 1 mM for the high affinity and low affinity components, respectively. Disulfides other than GSSG were also found to stimulate ATP hydrolysis. The similarity between the kinetic properties of the GSSG-stimulated ATPase and those reported for GSSG transport in erythrocytes suggests that the ATPase may function in the active extrusion of intracellular GSSG.
Lingua originale | Inglese |
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pagine (da-a) | 1999-2002 |
Numero di pagine | 4 |
Rivista | Journal of Biological Chemistry |
Volume | 260 |
Numero di pubblicazione | 4 |
Stato di pubblicazione | Pubblicato - 1985 |
Pubblicato esternamente | Sì |