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- Tamás Keleti
- 2012

We prove that a compact metric space (or more generally an analytic subset of a complete separable metric space) of Hausdorff dimension bigger than k can be always mapped onto a k-dimensional cube by a Lipschitz map. We also show that this does not hold for arbitrary separable metric spaces. As an application we essentially answer a question of Urbański by… (More)

- Tamás Keleti, Judit Ovádi, József Batke
- Progress in biophysics and molecular biology
- 1989

- Tamás Keleti
- 2008

For any countable collection of sets of three points we construct a compact subset of the real line with Hausdorff dimension 1 that contains no similar copy of any of the given triplets.

- M S Telegdi, Tamás Keleti
- Enzymologia
- 1966

- Judit Ovádi, Tamás Keleti
- European journal of biochemistry
- 1978

The possibility of interaction between purified rabbit muscle aldolase and D-glyceraldehyde-3-phosphate dehydrogenase was studied by rapid kinetic methods, by analyzing the kinetics of the consecutive reaction catalyzed by the coupled enzyme system. The Km of the intermediary product, glyceraldehyde 3-phosphate, produced by aldolase was determined in the… (More)

- Judit Ovádi, József Batke, Ferenc A. Bartha, Tamás Keleti
- Archives of biochemistry and biophysics
- 1979

- Judit Ovádi, M S Telegdi, József Batke, Tamás Keleti
- European journal of biochemistry
- 1971

- Judit Ovádi, Costantino Salerno, Tamás Keleti, P. M. Fasella
- European journal of biochemistry
- 1978

Polarization of fluorescence measurements of aldolase and D-glyceraldehyde-3-phosphate dehydrogenase labeled with fluorescein isothiocyanate have been used to detect the possible formation of a soluble complex between the proteins. The results suggest an interaction between aldolase and D-glyceraldehyde-3-phosphate dehydrogenase with an apparent… (More)

- Tamás Keleti, G. Rickey Welch
- The Biochemical journal
- 1984

Evolution of the kinetic potential of enzyme reactions is discussed. Quantitative assessment of the evolution of enzyme action has usually focused on optimization of the parametric ratio kcat./Km, which is the apparent second-order rate constant for the reaction of free substrate with free enzyme to give product. We propose that the general form… (More)

- Tamás Keleti, Judit Ovádi
- Current topics in cellular regulation
- 1988