Article
Properties of a recombinant human hemoglobin double mutant: sickle hemoglobin with Leu-88(beta) at the primary aggregation site substituted by Ala.
Protein science : a publication of the Protein Society - 1 Aug 1994
Martin de Llano J J, Manning J M
Abstract excerpt
A recombinant double mutant of hemoglobin (Hb), E6V/L88A(beta), was constructed to study the strength of the primary hydrophobic interaction in the gelation of sickle Hb, i.e., that between the mutant Val-6(beta) of one tetramer and the hydrophobic region between Phe-85(beta) and Leu-88(beta) on...
Topics
- Alanine
- Amino Acid Sequence
- Chemical Phenomena
- Chemistry, Physical
- Circular Dichroism
- Gels
- Globins
- Hemoglobin, Sickle
- Humans
- Isoelectric Focusing
- Leucine
- Macromolecular Substances
- Mass Spectrometry
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Oxygen
- Recombinant Proteins