Kinetic studies of chromaffin granule H+-ATPase and effects of bafilomycin A1
- 31 July 1990
- journal article
- Published by Elsevier BV in Biochemical and Biophysical Research Communications
- Vol. 170 (2), 873-878
- https://doi.org/10.1016/0006-291x(90)92172-v
Abstract
Vacuolar type H+-ATPase purified from bovine chromaffin granules did not show simple Michaelis-Menten type kinetics, and had apparent Km values of 5 μM, 30 μM and 300 μM. These three Km values suggested the presence of catalytic cooperativity during steady-state hydrolysis. The single turnover rate was 10−3 -fold the maximal velocity of the enzyme and similar to the rate estimated from the velocity of steady-state hydrolysis with the smallest Km value (5 μM). The H+-ATPase was inhibited by the stoichiometric binding of bafilomycin A1, a specific inhibitor of vacuolar type H+-ATPase. This inhibitor not only lowered the rate of ATP hydrolysis at the single catalytic site, but also affected the catalytic cooperativity of the enzyme.Keywords
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