Article
Preparation and kinetic characterization of a series of betaW37 variants of human hemoglobin A: evidence for high-affinity T quaternary structures.
Biochemistry - 31 Mar 1998
Kwiatkowski L D, Hui H L, Wierzba A, Noble R W, Walder R Y, Peterson E S, Sligar S G, Sanders K E
Abstract excerpt
Four variants of human beta globin in which the Trp at position 37 has been replaced with a Tyr, Ala, Gly, or Glu have been expressed in Escherichia coli. These globins have been combined with normal human alpha chains and heme to form tetrameric hemoglobin molecules. A technique for the preparation of alpha chain dimers, which are cross-linked between their alpha99 lysine residues, has been developed, and these...
Topics
- Amino Acid Substitution
- Carbon Monoxide
- Cross-Linking Reagents
- Escherichia coli
- Globins
- Hemoglobin A
- Humans
- Hydrogen-Ion Concentration
- Kinetics
- Mass Spectrometry