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Kinetics of Na+-ATPase: influence of Na+ and K+ on substrate binding and hydrolysisLiselotte Plesner; Igor W. Plesner · 1985
Purification and steady state kinetic mechanism of glycogen synthase-D from human polymorpho-nuclear leukocytesLiselotte Plesner; Igor W. Plesner; Viggo Esmann · 1976
Kinetics of (Na+ + K+)-ATPase: analysis of the influence of Na+ and K+ by steady-state kineticsIgor W. Plesner; Liselotte Plesner · 1985
Distinction between the intermediates in Na+-ATPase and Na+,K+-ATPase reactions. II. Exchange and hydrolysis kinetics at micromolar nucleotide concentrationsLiselotte Plesner; Igor W. Plesner · 1988
Distinction between the intermediates in Na+-ATPase and Na+,K+-ATPase reactions. I. Exchange and hydrolysis kinetics at millimolar nucleotide concentrationsLiselotte Plesner; Igor W. Plesner · 1988
The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain IV. Rate constant determinationIgor W. Plesner; Liselotte Plesner · 1981
The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain III. A minimal modelIgor W. Plesner; Liselotte Plesner; Jens G. Nørby; Irena Klodos · 1981