Characterization of Bovine Brain ATPase
Abstract
The purified bovine brain ATPase has been shown to be a high- affinity, low capacity pump, and consists of two proteins. A labile, high affinity dihydropyridine receptor activity has been associated with this ATPase activity. This study has shown that the purified (Ca2+ + Mg2+)-dependent ATPase can be immobilized, and that changes can be detected on the surface as increases in phosphate released and/or capacitance differences after interaction of the complex with a test ligand.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 1988
- Accession Number
- ADA198212
Entities
People
- James J. Valdes
- James P. Chambers
Organizations
- University of Texas at San Antonio