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. 1974 Apr;71(4):1504–1505. doi: 10.1073/pnas.71.4.1504

Chemical Modifications That Inhibit Gelation of Sickle Hemoglobin

Reinhold Benesch 1, Ruth E Benesch 1, Suzanna Yung 1
PMCID: PMC388258  PMID: 4524653

Abstract

Substitution of the N-terminal amino groups with pyridoxal compounds inhibits gelation and increases the solubility of deoxy sickle hemoglobin (Hb S). Pyridoxylation of the α chains has considerably more effect than that of the β chains. The increase in minimum gelling concentration of Hb S that results from modification of the α N-termini is the same as that produced by dilution of Hb S with an equal amount of Hb A.

Keywords: α and β N-terminal amino groups, pyridoxal phosphate, pyridoxal sulfate, hemoglobin solubility

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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