Functional size analysis of F-ATPase from Escherichia coli by radiation inactivation

• Published in: The Journal of biological chemistry Vol. 268; no. 15; pp. 10802 - 10807
• Main Authors: Ma, J.T., Wu, J.J., Tzeng, C.M., Pan, R.L.
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 25.05.1993; American Society for Biochemistry and Molecular Biology
• Subjects: Adenosine Triphosphate - metabolism; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Cell Membrane - enzymology; Cobalt Radioisotopes; Dose-Response Relationship, Radiation; Enzymes and enzyme inhibitors; Escherichia coli; Escherichia coli - enzymology; Fundamental and applied biological sciences. Psychology; Gramicidin - pharmacology; Hydrolases; Ionophores - pharmacology; Kinetics; Molecular Weight; Proton-Translocating ATPases - chemistry; Proton-Translocating ATPases - metabolism; Proton-Translocating ATPases - radiation effects; Thermodynamics; Valinomycin - pharmacology; Enzymatic activity; Molecular structure; Enzyme; Escherichia coli; Irradiation; Reaction mechanism; Bacteria; F0F1-ATPase; Inactivation; Molecular weight; Enterobacteriaceae

A radiation inactivation technique was employed to determine the functional size of adenosine triphosphatase from Escherichia coli (EF0EF1-ATPase). Functional units of the membrane-bound and the soluble ATPases were estimated to be 300 +/- 39 and 295 +/- 32 kDa, respectively. The presence of the fre...