[[abstract]]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-depleted ATPase moiety involved in ATP hydrolysis reaction was also determined. When both purified beta subunit and beta-depleted chromatophore were irradiated separately, reconstituted, and then activity measured, the functional mass was 312 +/- 50 kDa. Our compelling evidence directly indicates that three functional copies of beta subunits were required for ATP hydrolysis.[[fileno]]2050111010046[[department]]生科
AbstractAt saturating concentrations of ATP, soluble F1 from the Rhodospirillum rubrum (RF1) exhibit...
The resolution-reconstitution approach has been employed in order to gain information as to the subu...
The resolution-reconstitution approach has been employed in order to gain information as to the subu...
AbstractThe functional molecular masses of the vacuolar membrane H+-ATPase in Saccharomyces cerevisi...
AbstractA radiation inactivation technique was employed to determine the functional size of pyrophos...
AbstractAn αβ heterodimer of the F1-ATPase of Rhodospirillum rubrum was isolated by extraction of ch...
[[abstract]]A radiation inactivation technique was employed to determine the functional size of aden...
SIGLEAvailable from British Library Document Supply Centre-DSC:D199171 / BLDSC - British Library Doc...
AbstractA radiation inactivation technique was employed to determine the functional size of pyrophos...
AbstractThe functional molecular masses of the vacuolar membrane H+-ATPase in Saccharomyces cerevisi...
AbstractEndogenous protein phosphorylation in cellular fractions from Rhodospirillum rubrum was mani...
AbstractF0F1-ATP synthase (H+-ATP synthase, F0F1) utilizes the transmembrane protonmotive force to c...
ABSTRACT: A survey of RuvB protein-mediated ATP hydrolysis yields the following observations. (1) Th...
none8Abstract H+-FOF1-ATP synthase couples proton flow through its membrane portion, FO, to the syn...
A1AO ATP synthases couple ion-transport of the AO sector and ATP synthesis/hydrolysis of the A3B3-he...
AbstractAt saturating concentrations of ATP, soluble F1 from the Rhodospirillum rubrum (RF1) exhibit...
The resolution-reconstitution approach has been employed in order to gain information as to the subu...
The resolution-reconstitution approach has been employed in order to gain information as to the subu...
AbstractThe functional molecular masses of the vacuolar membrane H+-ATPase in Saccharomyces cerevisi...
AbstractA radiation inactivation technique was employed to determine the functional size of pyrophos...
AbstractAn αβ heterodimer of the F1-ATPase of Rhodospirillum rubrum was isolated by extraction of ch...
[[abstract]]A radiation inactivation technique was employed to determine the functional size of aden...
SIGLEAvailable from British Library Document Supply Centre-DSC:D199171 / BLDSC - British Library Doc...
AbstractA radiation inactivation technique was employed to determine the functional size of pyrophos...
AbstractThe functional molecular masses of the vacuolar membrane H+-ATPase in Saccharomyces cerevisi...
AbstractEndogenous protein phosphorylation in cellular fractions from Rhodospirillum rubrum was mani...
AbstractF0F1-ATP synthase (H+-ATP synthase, F0F1) utilizes the transmembrane protonmotive force to c...
ABSTRACT: A survey of RuvB protein-mediated ATP hydrolysis yields the following observations. (1) Th...
none8Abstract H+-FOF1-ATP synthase couples proton flow through its membrane portion, FO, to the syn...
A1AO ATP synthases couple ion-transport of the AO sector and ATP synthesis/hydrolysis of the A3B3-he...
AbstractAt saturating concentrations of ATP, soluble F1 from the Rhodospirillum rubrum (RF1) exhibit...
The resolution-reconstitution approach has been employed in order to gain information as to the subu...
The resolution-reconstitution approach has been employed in order to gain information as to the subu...