A Comparison of the Resistance of Human and Horse Ferrihemoglobin to Acid Denaturation
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference28 articles.
1. Kinetic Study of the Reversible Acid Denaturation of Ferrihemoglobin1
2. Effect of Temperature on the Reversible pH-dependent Denaturation of Horse Ferrihemoglobin1
3. Kinetic and Equilibrium Measurements of the Regeneration of Acid-denatured Horse Ferrihemoglobin1
4. Distinct Reversibly Denatured Ferrihemoglobins Produced at pH 3.51
5. Increase in Acid-binding Sites on Denaturation of Horse Ferrihemoglobin at 0°1
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1. Carbodiimide EDC Induces Cross-Links That Stabilize RNase A C-Dimer against Dissociation: EDC Adducts Can Affect Protein Net Charge, Conformation, and Activity;Bioconjugate Chemistry;2009-07-16
2. Alkaline Denaturation of Ferrihemoglobins A, S and C;European Journal of Biochemistry;1974-11
3. Comparison of the acid denaturation of several hemoglobins which differ in amino acid sequence;Archives of Biochemistry and Biophysics;1974-04
4. Interaction of Human Hemoglobin with Haptoglobin or Antihemoglobin Antibody;Journal of Biological Chemistry;1974-04
5. Kinetics of unfolding and refolding of proteins;Journal of Molecular Biology;1973-01
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