High-resolution differential scanning calorimetric analysis of the subunits of Escherichia coli aspartate transcarbamoylase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00342a032
Reference44 articles.
1. Calorimetric analysis of aspartate transcarbamylase from Escherichia coli. Binding of cytosine 5'-triphosphate and adenosine 5'-triphosphate
2. Bohr effect of Escherichia coli aspartate transcarbamylase. Linkages between substrate binding, proton binding, and conformational transitions
3. Alteration of the allosteric properties of aspartate transcarbamoylase by pyridoxylation of the catalytic and regulatory subunits
4. Assembly of the catalytic trimers of aspartate transcarbamoylase from folded monomers.
5. Interactions of ionizable groups in E. coli aspartate transcarbamylase with adenosine and cytidine 5'-triphosphates
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