Abstract
1. The purification of an adenosine triphosphatase present in aqueous extracts of acetone-dried ox-heart mitochondria is described. 2. No evidence was found for the presence of more than one protein having adenosine-triphosphatase activity in these extracts. 3. The enzyme is less stable at 0° than at 25° but is stabilized by glycerol. 4. The activity is dependent on the presence of Mg2+ or certain other bivalent metal cations. 5. The adenosine-triphosphatase activity of the Mg2+-activated enzyme is enhanced by 2,4-dinitrophenol. 6. The kinetics of Mg2+ activation indicate that the ATP–Mg2+ complex is the important substrate: free ATP and Mg2+ are inhibitory. 7. This preparation of mitochondrial adenosine triphosphatase has many properties in common with the adenosine triphosphatase coupling factor from mitochondria (Racker, 1961).
Dates
Type | When |
---|---|
Created | 10 years ago (Aug. 13, 2015, 5:36 p.m.) |
Deposited | 3 years, 8 months ago (Nov. 29, 2021, 3:37 p.m.) |
Indexed | 1 year, 8 months ago (Dec. 11, 2023, 1:58 a.m.) |
Issued | 57 years, 10 months ago (Oct. 1, 1967) |
Published | 57 years, 10 months ago (Oct. 1, 1967) |
Published Print | 57 years, 10 months ago (Oct. 1, 1967) |
@article{Selwyn_1967, title={Preparation and general properties of a soluble adenosine triphosphatase from mitochondria}, volume={105}, ISSN={0306-3283}, url={http://dx.doi.org/10.1042/bj1050279}, DOI={10.1042/bj1050279}, number={1}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Selwyn, M J}, year={1967}, month=oct, pages={279–288} }