Radiation inactivation analysis of chloroplast CF0-CF1 ATPase

Radiation inactivation technique was employed to measure the functional size of adenosine triphosphatase of spinach chloroplasts. The functional size for acid-base-induced ATP synthesis was 450 +/- 24 kilodaltons; for phenazine methosulfate-mediated ATP synthesis, 613 +/- 33 kilodaltons; and for met...

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Bibliographic Details
Published in:The Journal of biological chemistry 1988-06, Vol.263 (18), p.8838-8843
Main Authors: Wang, M Y, Chien, L F, Pan, R L
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - antagonists & inhibitors
Adenosine Triphosphatases - radiation effects
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Ca(2+) Mg(2+)-ATPase - metabolism
Calcium-Transporting ATPases - metabolism
Chloroplasts - enzymology
Dose-Response Relationship, Radiation
Enzyme Activation
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
HIDROLASAS
HYDROLASE
HYDROLASES
Intracellular Membranes - enzymology
Kinetics
Plants - enzymology
PLASTE
PLASTIDIOS
PLASTIDS
RADIACIONES
RADIATION
RADIATIONS
SPINACIA OLERACEA
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Summary:Radiation inactivation technique was employed to measure the functional size of adenosine triphosphatase of spinach chloroplasts. The functional size for acid-base-induced ATP synthesis was 450 +/- 24 kilodaltons; for phenazine methosulfate-mediated ATP synthesis, 613 +/- 33 kilodaltons; and for methanol-activated ATP hydrolysis, 280 +/- 14 kilodaltons. The difference (170 +/- 57 kilodaltons) between 450 +/- 24 and 280 +/- 14 kilodaltons is explained to be the molecular mass of proton channel (coupling factor 0) across the thylakoid membrane. Our data suggest that the stoichiometry of subunits I, II, and III of coupling factor 0 is 1:2:15. Ca2+- and Mg2+-ATPase activated by methanol, heat, and trypsin digestion have a similar functional size. However, anions such as SO3(2-) and CO3(2-) increased the molecular mass for both ATPase's (except trypsin-activated Mg2+-ATPase) by 12-30%. Soluble coupling factor 1 has a larger target size than that of membrane-bound. This is interpreted as the cold effect during irradiation.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)68383-8