Isolation of a highly active H+-ATPase from beef heart mitochondria
- 1 December 1982
- journal article
- research article
- Published by Springer Nature in Journal of Bioenergetics and Biomembranes
- Vol. 14 (5-6) , 287-295
- https://doi.org/10.1007/bf00743058
Abstract
The lysolecithin extraction procedure originally described by Sadleret al. (1974) has been modified to yield a H+-ATPase with high levels of Pi-ATP exchange activity (400–600 nmol × min−1 × mg−1). This activity is further enhanced (1400–1600 nmol × min−1 × mg−1) following sucrose density gradient centrifugation in the presence of asolectin. This enhancement results in part from a lipid-dependent activation and in part from removal of inactive complexes. The H+ translocating activity of the complex has been determined spectrophotometrically using binding of oxonol VI as an indicator of membrane potential. Pi-ATP exchange, ATP hydrolysis, and oxonol binding are sensitive to energy-transfer inhibitors (oligomycin, rutamycin) and/or uncouplers (DNP, FCCP).Keywords
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