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The Journal of Biological Chemistry|March 25, 1977
Interactions of phospho- and dephosphosuccinyl coenzyme A synthetase with manganous ion and substrates. Studies of manganese complexes by NMR relaxation rates of water protonsD H Buttlaire, M ChonThe Journal of Biological Chemistry|January 10, 1975
Electron paramagnetic resonance and water proton relaxation rate studies of formyltetrahydrofolate synthetase-manganous ion complexes. Evidence for involvement of substrates in the promotion of a catalytically competent active siteD H Buttlaire, G H Reed, R HimesThe Journal of Biological Chemistry|November 25, 1976
31P NMR studies of the arginine kinase reaction. Equilibrium constants and exchange rates at stoichiometric enzyme concentrationB D Rao, D H Buttlaire, M CohnThe Journal of Biological Chemistry|July 10, 1976
Formyltetrahydrofolate synthetase-catalyzed formation of ATP from carbamyl phosphate and ADP. Evidence for a formyl phosphate intermediate in the enzyme's catalytic mechanismD H Buttlaire, R H Himes, G H ReedThe Journal of Biological Chemistry|January 10, 1975
Equilibrium and water proton relaxation rate enhancement properties of formyltetrahydrofolate synthetase-manganous ion-substrate complexesD H Buttlaire, G H Reed, R H HimesBiochimica Et Biophysica Acta|April 12, 1979
Carbamyl phosphate-dependent ATP synthesis catalyzed by formyltetrahydrofolate synthetaseD H Buttlaire, C A Balfe, M F Wendland, et al.Biochemistry|February 15, 1983
Nuclear magnetic resonance studies of formyltetrahydrofolate synthetase interactions with formate and methylammonium ionM F Wendland, T H Stevens, D H Buttlaire, et al.The Journal of Biological Chemistry|March 10, 1980
Manganous ion binding to tubulinD H Buttlaire, B A Czuba, T H Stevens, et al.Pageof 1