Article
The heme-globin and dimerization equilibria of recombinant human hemoglobins carrying site-specific beta chains mutations.
Archives of biochemistry and biophysics - 15 Feb 2001
Gattoni M, Piro M C, Boffi A, Brinigar W S, Fronticelli C, Chiancone E
Abstract excerpt
The heme-globin and dimer-tetramer equilibria of ferric recombinant human hemoglobins with site-specific beta chain mutations at the heme pocket or at either the a1beta1 or the alpha1beta2 interfaces have been determined. The heme pocket mutation V67T leads to a marked stabilization of the beta chain heme and does not affect the dimer-tetramer association constant, K2,4. In the C112 mutants, the intrinsic rate of...
Topics
- Albumins
- Amino Acid Substitution
- Binding Sites
- Chromatography, Gel
- Dimerization
- Heme
- Hemoglobins
- Humans
- Hydrogen-Ion Concentration
- Kinetics
- Mutagenesis, Site-Directed