USE OF HPLC FOR THE STUDY OF ADP BINDING TO CHLOROPLAST ATPase. II. ITS EFFECT ON ENZYMATIC ACTIVITY
Author:
Affiliation:
1. a CEA Saclay , Section de Bioenergetique, Gif sur Yvette Cedex, F-91191, France
Publisher
Informa UK Limited
Subject
Clinical Biochemistry,Pharmaceutical Science,Biochemistry,Analytical Chemistry
Link
https://www.tandfonline.com/doi/pdf/10.1081/JLC-100100441
Reference42 articles.
1. Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
2. The 2.8-A structure of rat liver F1-ATPase: Configuration of a critical intermediate in ATP synthesis/hydrolysis
3. Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants for elementary steps in catalysis at a single site.
4. Adenine nucleotide binding sites on beef heart F1-ATPase. Asymmetry and subunit location.
5. Catalytic site occupancy during ATP hydrolysis by MF1-ATPase. Evidence for alternating high affinity sites during steady-state turnover.
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1. Use of the Hummel and Dreyer method for the study of nucleotide binding on chloroplast ATPase CF1;Journal of Chromatography B;2002-02
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