Calorimetric studies of the binding of ligands to aldolase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00739a012
Reference27 articles.
1. Calorimetric studies of the activation of chymotrypsinogen A
2. Calorimetric studies of protein-inhibitor interaction. I. Binding of 3'-cytidine monophosphate to ribonuclease A at pH 5.5
3. The binding-sites of rabbit muscle aldolase
4. Ultraviolet difference spectroscopic studies of the binding of ligands to rabbit muscle aldolase
5. Specific Anion Binding to Fructose Diphosphate Aldolase from Rabbit Muscle*
Cited by 11 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Thermodynamics of the binding of chymotrypsin with the black-eyed pea trypsin and chymotrypsin inhibitor (BTCI);Journal of Protein Chemistry;1999
2. Thermodynamic Data for Protein-Ligand Interaction;Thermodynamic Data for Biochemistry and Biotechnology;1986
3. Interaction of Fructose- 1,6-Bisphosphate Aldolase with Adenine Nucleotides. Binding of 5'-Mononucleotides and Phosphates to Rabbit Muscle Aldolase;European Journal of Biochemistry;1980-03
4. The Thermodynamics of Nucleotide Binding to Protein;Critical Reviews in Biochemistry;1980-01
5. Rabbit muscle myogen. Interactions with phosphate as the source of non-enantiography in moving-boundary electrophoresis;Biochemical Journal;1976-09-01
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