Calorimetric Demonstration of the Potential of Molecular Crowding To Emulate the Effect of an Allosteric Activator on Pyruvate Kinase Kinetics
Author:
Affiliation:
1. Department of Biochemistry, School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Queensland 4072, Australia
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi020064h
Reference27 articles.
1. Space-filling effects of inert solutes as probes for the detection and study of substrate-mediated conformational changes by enzyme kinetics: Theoretical considerations
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