Purine nucleoside phosphorylase of rabbit liver. Mechanism of catalysis.
Open Access
- 1 January 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (2) , 732-738
- https://doi.org/10.1016/s0021-9258(17)32779-5
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- The kinetics of enzyme-catalyzed reactions with two or more substrates or products: II. Inhibition: Nomenclature and theoryPublished by Elsevier ,2003
- Use of chromium-adenosine triphosphate and lyxose to elucidate the kinetic mechanism and coordination state of the nucleotide substrate for yeast hexokinaseBiochemistry, 1975
- A trimeric structure for mammalian purine nucleoside phosphorylaseFEBS Letters, 1973
- The kinetics of enzyme-catalyzed reactions with two or more substrates or productsBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963
- On the Determination of Rate Constants for Coenzyme Mechanisms1Journal of the American Chemical Society, 1958
- Graphical determination of the dissociation constants for two-substrate enzyme systemsBiochimica et Biophysica Acta, 1957
- Initial Steady State Velocities in the Evaluation of Enzyme-Coenzyme-Substrate Reaction Mechanisms.Acta Chemica Scandinavica, 1957
- The Relationship between Michaelis Constants, Maximum Velocities and the Equilibrium Constant for an Enzyme-catalyzed ReactionJournal of the American Chemical Society, 1953
- Studies on Liver Alcohol Dehydrogenase. II. The Kinetics of the Compound of Horse Liver Alcohol Dehydrogenase and Reduced Diphosphopyridine Nucleotide.Acta Chemica Scandinavica, 1951
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934