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Heparin interacts with a selenoprotein in human plasma
1Department of Clinical Chemistry, University Hospital, University of Lund, Sweden.
Journal of Inorganic Biochemistry
|August 1, 1988
Summary
Heparin in plasma interacts with a major selenium-binding protein, altering its size during chromatography. This interaction, blocked by protamine, explains differences in selenium distribution observed with various anticoagulants.
Area of Science:
- Biochemistry
- Analytical Chemistry
- Clinical Chemistry
Background:
- Selenium is an essential trace element crucial for various physiological functions.
- The distribution and binding of selenium in human plasma can be influenced by experimental conditions.
- Previous studies reported discrepancies in selenium distribution, potentially due to anticoagulant use.
Purpose of the Study:
- To investigate the interaction between heparin and selenium-containing proteins in human plasma.
- To elucidate the cause of differing selenium distribution patterns observed with various anticoagulants.
Main Methods:
- Gel filtration chromatography (Sephadex G-150) of human serum and heparinized plasma.
- Analysis of selenium-containing peaks and their elution profiles (Kav values).
- Assessment of heparin's effect using protamine sulfate.
Main Results:
- A major selenium-containing protein peak showed a different elution profile (Kav 0.19 in serum vs. 0.01 in heparinized plasma).
- This shift indicated a strong interaction between heparin and the selenium-binding protein.
- Protamine sulfate, a heparin antagonist, abolished the heparin-induced shift.
- The identified heparin-interacting protein was distinct from glutathione peroxidase.
Conclusions:
- Heparin in plasma directly interacts with a major selenium-containing protein.
- This interaction alters the protein's apparent size during gel filtration chromatography.
- The findings reconcile previous discrepancies in plasma selenium distribution related to anticoagulant choice.