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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Kinetics of polymerization of hemoglobin S modified by thiol reagents and by oxidation.

The effects of four thiol reagents on the kinetics of polymerization of hemoglobin S have been studied in high phosphate buffer (1.8 M), in the presence (3 mM) or absence of sodium dithionite, depending on the reduction of mixed disulfides of Hb in the presence of this reducing agent. The effect of oxidized forms (methemoglobin) of HbS on the kinetics of aggregation of deoxyHbS was also studied because of the presence of 33% metHbS when HbS was modified by 4-aminophenyl disulfide. In the presence of sodium dithionite, the delay times prior to polymerization of deoxyHbS modified by N-ethylmaleimide, iodoacetamide and 4-aminophenyl disulfide were, respectively, 1.5-, 1.35- and 1.15-times longer than that of native deoxyHbS. The results indicate that the radicals bound to the cysteine beta 93 residue inhibit the contacts in the polymer formation to various extents but do not modify the size of the nuclei.[1]

References

  1. Kinetics of polymerization of hemoglobin S modified by thiol reagents and by oxidation. Domenget, C., Garel, M.C., Rhoda, M.D., Caburi-Martin, J., Galacteros, F., Beuzard, Y. Biochim. Biophys. Acta (1985) [Pubmed]
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