EurekaMag.com logo
+ Site Statistics
References:
47,893,527
Abstracts:
28,296,643
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Radiation inactivation analysis of chloroplast CF0-CF1 ATPase


, : Radiation inactivation analysis of chloroplast CF0-CF1 ATPase. Journal of Biological Chemistry 263(18): 8838-8843

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 SO32- and CO32- 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.


Accession: 001667702

PMID: 2967817

Submit PDF Full Text: Here


Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:
Close
Close

Related references

Wang M.Y.; Chien L.F.; Pan R.L., 1988: Radiation inactivation analysis of chloroplast cf o cf 1 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-media...

Rabon, E.C.; Gunther, R.D.; Bassilian, S.; Kempner, E.S., 1988: Radiation inactivation analysis of oligomeric structure of the H,K-ATPase. The oligomeric size of the H,K-ATPase was determined in frozen gastric microsomal vesicles irradiated with high energy electrons. Target sizes of various catalytic activities associated with H,K-ATPase function fell into two distinct groups. The l...

Sarafian, V.P.tier, M.P.ole, R., 1992: Radiation-inactivation analysis of vacuolar H+-ATPase and H+-pyrophosphatase from Beta vulgaris L. The functional sizes of the vacuolar H+-ATPase (V-ATPase: EC 3.6.1.34) and H+-pyrophosphatase (PPase; EC 3.6.1.1) from vacuolar membranes of red beet (Beta vulgaris L.) were estimated by radiation inactivation, both for substrate hydrolysis and fo...

Ma, J.T.; Wu, J.J.; Tzeng, C.M.; Pan, R.L., 1993: Functional size analysis of F-ATPase from Escherichia coli by radiation inactivation. A radiation inactivation technique was employed to determine the functional size of adenosine triphosphatase from Escherichia coli (EF-0EF-1-ATPase). Functional units of the membrane-bound and the soluble ATPases were estimated to be 300 +- 39 and...

Rabon E.C.; Gunther R.D.; Bassilian S.; Kempner E.S., 1988: Radiation inactivation analysis of oligomeric structure of the proton potassium atpase. The oligomeric size of the H,K-ATPase was determined in frozen gastric microsomal vesicles irradiated with high energy electrons. Target sizes of various catalytic activities associated with H,K-ATPase function fell into two distinct groups. The l...

Schrijen, J.J.; Van Groningen-Luyben, W.A.; Nauta, H.; D.P.nt, J.J.; Bonting, S.L., 1983: Studies on (K+ + H+)-ATPase. VI. Determination on the molecular size by radiation inactivation analysis. (1) A (K+ + H+)-ATPase containing membrane fraction, isolated from pig gastric mucosa, has been further purified by means of zonal electrophoresis, leading to a 20% increase in specific activity and an increase in ratio of (K+ + H+)-ATPase to basa...

Schrijen, J.J.; Van-Groningen-Luyben, W.A.H.M.; Nauta, H.; De-Pont, J.J.H.H.M.; Bonting, S.L., 1983: Potassium proton atpase 4. determination of the molecular size by radiation inactivation analysis. A (K++H+)-ATPase containing membrane fraction, isolated from pig gastric mucosa, was further purified by zonal electrophoresis, leading to a 20% increase in specific activity and an increase in ratio of (K++H+)-ATPase to basal Mg2+-ATPase activity...

Mal'ian, A.N., 1981: Inactivation of chloroplast CF1-ATPase. Inactivation of chloroplasts ATPase at alkalization of the medium and under the effect of chaotropic reagent (NaBr) was studied. An increase of the enzyme solution pH was accompanied with an increase of optical density with the wavelength 294 nm d...

Chien, L.F.; Wu, J.J.; Tzeng, C.M.; Pan, R.L., 1993: ATPase of Rhodospirillum rubrum requires three functional copies of beta subunit as determined by radiation inactivation analysis. Radiation inactivation analysis yielded a functional unit of 170 +/- 26 kDa as beta subunit of ATPase was irradiated and then reconstituted to beta-depleted chromatophores of Rhodospirillum rubrum. A functional size of 132 +/- 17 kDa for the beta-...

Hirata, R.; Ohsumi, Y.; Anraku, Y., 1989: Functional molecular masses of vacuolar membrane H+-ATPase from Saccharomyces cerevisiae as studied by radiation inactivation analysis. The functional molecular masses of the vacuolar membrane H+-ATPase in Saccharomyces cerevisiae under two kinetic conditions for ATP hydrolysis were measured by radiation inactivation. When vacuolar membrane vesicles were exposed to gamma-rays from...