Apr 14, 1976

Interaction of serum albumin with normal and sickle hemoglobins

Biochimica Et Biophysica Acta
K Adachi, T Asakura

Abstract

The stability of oxyhemoglobin S during mechanical shaking was enhanced by the addition of human serum albumin. The stabilizing effect was maximum when the concentration of serum albumin approached that of oxyhemoglobin, suggesting a molecular level interaction between them. The effects of serum albumin on oxyhemoglobin A were essentially similar to those on oxyhemoglobin S. Deoxy- and methemoglobins were also stabilized by serum albumin. The addition of human serum albumin to a solution containing sickle cell oxyhemoglobin slowly formed a compound which had an absorbance peak at 620 nm. After purification by Sephadex G-200 column chromatography, this compound was identified as methemalbumin. Comparison of the rates of formation of methemalbumin from hemoglobin with various ligand states and human serum albumin showed that the rate of formation from hemichrome was much faster than from met-, oxy- and deoxyhemoglobin. About 60% of the heme was transferred from hemichrome to albumin when the mixture was kept standing at room temperature for 5 min, in contrast to only 5% from methemoglobin. This result suggests that hemichrome, rather than methemoglobin, is the intermediate in the formation of methemalbumin from oxyhemoglobin and ...Continue Reading

  • References4
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References

  • References4
  • Citations2

Citations

Mentioned in this Paper

Serum Albumin Measurement
Macromolecular Compounds
Sephadex G 200
Deoxyhemoglobin
Methemoglobin
Methemalbumin Assay
ALB
Albumin Human, USP
Human Serum Albumin [EPC]
Hemoglobin SS

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