Effect of structural perturbations on the ligand-binding properties of human methemoglobin A.
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Bromides↗
Biomedical subjects
M H Klapper
Publications and source records attributed to M H Klapper.
Nonequivalent binding to human methemoglobin. Thermodynamic and kinetic comparison.
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Binding Sites↗
Evidence for nonequivalent binding sitesin human methemoglobin.
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Binding Sites↗
On the nature of the protein interior.
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Amino Acids↗
The reaction of p-mercuribenzoate with methemerythrin.
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Benzoates↗
Evidence for an irreversible reaction between nitrite and human methemoglobin.
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Chemical Phenomena↗
Three new iron-ligand complexes of human methemoglobin A.
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Bromides↗
Rapid binding of PMB to non-SH groups on hemerythrin.
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Animals↗
Cooperative interactions and determination of protein association-dissociation equilibria. Hemerythrin.
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Binding Sites↗
Evidence from sedimentation velocity for dissociation equilibrium in hemerythrin.
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Chemical Phenomena↗
Hybridization experiments: evidence of dissociation equilibrium in hemerythrin.
Partial succinylation of hemerythrin alters its electrophoretic mobility even though it remains an octameric macromolecule. Mixtures of this modified protein and unmodified hemerythrin generate species of intermediate electrophoretic mobility. Such behavior provides strong evidence that the octameric macromolecule is in mobile equilibrium with monomeric subunits.
Chemical Phenomena↗