Recombinant sickle hemoglobin containing a lysine substitution at Asp-85(alpha): expression in yeast, functional properties, and participation in gel formation.
Explore this paper's citation graph
Summary
A wide range of gelation values demonstrates that some sites are more important than others in promoting HbS aggregation, and Asp-85(alpha) is classified as a moderate contributor to the strength of the HBS aggregate.
- Type
- article
- Published
- 1997-06-01
- Cited by
- 7
- References
- 55
- Access
- Open access
- OpenAlex
- https://openalex.org/W16528690
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:1868510
Keywords
Chemistry, Hemoglobin, Cooperativity, Mutant, Recombinant DNA
References
- Enhanced survival of sickle erythrocytes upon treatment with glyceraldehyde.
- Preparation of hemoglobin carbamylated at specific NH2-terminal residues.
- alpha Chain mutations with opposite effects on the gelation of hemoglobin S.
- Methyl acetyl phosphate as a covalent probe for anion-binding sites in human and bovine hemoglobins.
- Role of hydrophobicity of phenylalanine beta 85 and leucine beta 88 in the acceptor pocket for valine beta 6 during hemoglobin S polymerization.
- Refined crystal structure of deoxyhemoglobin S. II. Molecular interactions in the crystal.
- X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A. Evidence for the location of a proton- and oxygen-linked chloride binding site at valine 1 alpha.
- Equilibrium oxygen binding to human hemoglobin cross-linked between the alpha chains by bis(3,5-dibromosalicyl) fumarate.
- Role of gamma 87 Gln in the inhibition of hemoglobin S polymerization by hemoglobin F.
- Oxygen-linked binding sites for inorganic anions to hemoglobin.
- The chloride effect in human haemoglobin. A new kind of allosteric mechanism.
- Sickle cell hemoglobin polymerization.
- Hemoglobin Atago (alpha2-85Tyr beta-2) a new abnormal human hemoglobin found in Nagasaki. Biochemical studies on hemoglobins and myoglobins. VI.
- Production of unmodified human adult hemoglobin in Escherichia coli.
- Factors affecting the ultraviolet laser desorption of proteins.
- Location and bond type of intermolecular contacts in the polymerisation of haemoglobin S
- Oxygen binding and other physical properties of human hemoglobin made in yeast.
- Properties of a recombinant human hemoglobin double mutant: Sickle hemoglobin with Leu‐88 (β) at the primary aggregation site substituted by Ala
- Participation and Strength of Interaction of Lysine 95(β) in the Polymerization of Hemoglobin S as Determined by Its Site-directed Substitution by Isoleucine (*)
- Synthesis of Wild Type and Mutant Human Hemoglobins in Saccharomyces cerevisiae
Cited by
- Sickle Cell Hemoglobin with Mutation at αHis-50 Has Improved Solubility*
- Linkage of Interactions in Sickle Hemoglobin Fiber Assembly
- A strategy for the generation of non‐aggregating mutants of Anthozoa fluorescent proteins
- Structural basis for the fast maturation of Arthropoda green fluorescent protein
- Recombinant hemoglobin variants.
Related papers
- Cat Hemoglobin: pH-Dependent Cooperativity of Oxygen Binding
- Theoretical investigation into the cooperativity effect of 1,4-dimethoxy-d-glucosamine complex with Na+ and H2O
- Utility function and cooperativity in binding systems
- Investigating cyclic cooperativity in ring stabilization of (HCN)n and (HNC)n: n = 3–11 clusters
- Interaction of organic phosphates with bovine hemoglobin
- Mechanism of cooperative oxygen binding to hemoglobin (spin-labeled triphosphate-concerted transition model-hemoglobin chesapeake).
- Role of Bohr group salt bridges in cooperativity in hemoglobin.