Molecular basis of ionic strength effects: interaction of enzyme and sulfate ion in carbon dioxide hydration and bicarbonate ion dehydration reactions catalyzed by carbonic anhydrase II
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00399a067
Reference38 articles.
1. A Study of the Variation of the Average Isoelectric Points of Several Plasma Proteins with Ionic Strength.
2. Study of Protein-Ion Interaction by the Moving Boundary Method. The Combination of Bovine Serum Albumin with Chloride Ion1
3. Alteration of the Kinetic Properties of an Enzyme by the Binding of Buffer, Inhibitor, or Substrate
4. Solvent Effects in the α-Chymotrypsin—Hydrocinnamic Ester System1
5. Evidence of exchangeable protons in the donor groups of the acidic form of cobalt bovine carbonic anhydrase B
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1. A high salt tolerant neutral protease from Aspergillus Oryzae: Purification, characterization and kinetic properties;Applied Biochemistry and Microbiology;2013-07
2. Comparison of solution and crystal properties of Co(II)–substituted human carbonic anhydrase II;Archives of Biochemistry and Biophysics;2010-10
3. Hofmeister effect on enzymatic catalysis and colloidal structures;Current Opinion in Colloid & Interface Science;2004-08
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