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Interaction of a macromolecular polyanion, dextran sulfate, with human hemoglobin
Author(s) -
Sacco Daniel,
Dellacherie Edith
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80490-2
Subject(s) - hemoglobin , chemistry , oxygen–haemoglobin dissociation curve , dextran , sulfate , oxygen , potentiometric titration , bohr effect , macromolecule , inorganic chemistry , binding site , dissociation (chemistry) , biophysics , biochemistry , organic chemistry , ion , biology
Interactions of dextran sulfate with amino groups of oxy‐ and deoxyhemoglobin were followed by both potentiometric measurements between pH 6 and 7.3 and oxygen‐binding studies. The uptake of protons observed upon addition of dextran sulfate to hemoglobin shows that the interaction with the deoxy form is strong and that the main site is probably located in the phosphate‐binding β‐cavity, whereas the interaction with the oxy form is more diffuse, probably with a great number of relatively weak binding sites. The influence of dextran sulfate on the oxygen dissociation curve of hemoglobin confirms these findings, as the effect of the polymer is to lower hemoglobin affinity for oxygen to a great extent, which proves that it stabilizes the deoxy form more strongly than the oxy one.