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August 23, 1988Biochemistry

Influence of ligation state and concentration of hemoglobin A on its crosslinking by glycolaldehyde: functional properties of crosslinked, carboxymethylated hemoglobin

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LMLois R. ManningNortheastern UniversityJMJames M. ManningCentre for Inflammation Research

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Manning et al. (1988) studied this question.

synapsesocial.com/papers/6aa770648fe5cf1d54fedc1bhttps://doi.org/10.1021/bi00417a064
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Selective carboxymethylation of the alpha-amino groups of hemoglobin. Effect on functional properties.1983 · 44 citations
  2. 2Reaction of glycolaldehyde with proteins: latent crosslinking potential of alpha-hydroxyaldehydes.1983 · 89 citations
  3. 3Oxygen-linked binding sites for inorganic anions to hemoglobin.1980 · 71 citations
  4. 4The specific influence of carbon dioxide and carbamate compounds on the buffer power and Bohr effects in human haemoglobin solutions1967 · 146 citations