inosine-triphosphate and chromium-adenosine-diphosphate

inosine-triphosphate has been researched along with chromium-adenosine-diphosphate* in 1 studies

Other Studies

1 other study(ies) available for inosine-triphosphate and chromium-adenosine-diphosphate

Article	Year
alpha, beta-Bidentate CrADP abolishes the negative cooperativity of yeast mitochondrial F1-ATPase. Biochimica et biophysica acta, 1985, Jan-23, Volume: 806, Issue:1 The hydrolysis of MgATP and MgITP by mitochondrial F1-ATPase from Saccharomyces cerevisiae is competitively inhibited by alpha, beta-CrADP, alpha, beta, gamma-CrATP and beta, gamma-CrATP. The apparent K1 values of the three complexes are in the range of the half-saturating MgATP concentration. The negative cooperativity (nH = 0.7) of MgATP hydrolysis is totally abolished by alpha, beta-CrADP (nH = 1.0), while it is not affected by the CrATP. It is concluded that alpha, beta-CrADP binds exclusively at the regulatory site and that CrATP binds exclusively to the catalytic site. Topics: Adenosine Diphosphate; Adenosine Triphosphate; Inosine Triphosphate; Kinetics; Proton-Translocating ATPases; Saccharomyces cerevisiae; Stereoisomerism	1985

Article

Year

alpha, beta-Bidentate CrADP abolishes the negative cooperativity of yeast mitochondrial F1-ATPase.

Biochimica et biophysica acta, 1985, Jan-23, Volume: 806, Issue:1

The hydrolysis of MgATP and MgITP by mitochondrial F1-ATPase from Saccharomyces cerevisiae is competitively inhibited by alpha, beta-CrADP, alpha, beta, gamma-CrATP and beta, gamma-CrATP. The apparent K1 values of the three complexes are in the range of the half-saturating MgATP concentration. The negative cooperativity (nH = 0.7) of MgATP hydrolysis is totally abolished by alpha, beta-CrADP (nH = 1.0), while it is not affected by the CrATP. It is concluded that alpha, beta-CrADP binds exclusively at the regulatory site and that CrATP binds exclusively to the catalytic site.

Topics: Adenosine Diphosphate; Adenosine Triphosphate; Inosine Triphosphate; Kinetics; Proton-Translocating ATPases; Saccharomyces cerevisiae; Stereoisomerism

1985