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The different forms of antithrombin II in serum
Thrombosis and Haemostasis
|August 31, 1977
Summary
Researchers isolated antithrombin III (AT III) complexes from human serum, finding evidence of polymeric forms and potential degradation products. This study advances understanding of AT III complex formation in biological systems.
Area of Science:
- Biochemistry
- Hematology
Background:
- Antithrombin III (AT III) is a key regulator of coagulation.
- Understanding the forms and complexes of AT III in serum is crucial for hemostasis research.
Purpose of the Study:
- To isolate and characterize antithrombin III (AT III) complexes from human serum.
- To investigate the molecular weight and potential polymeric nature of AT III complexes in vivo.
Main Methods:
- Affinity chromatography using heparin-agarose.
- Gel filtration chromatography.
- Radioactive labeling with 125I-thrombin to detect thrombin-AT III complexes.
Main Results:
- Complexed AT III bound less strongly to heparin-agarose than free AT III, with approximately 50% of AT III found free.
- A 2.5 x 10(5) molecular weight complex containing thrombin was isolated from serum.
- A 9 x 10(4) molecular weight complex was detected only in synthetic systems, not in serum, suggesting polymeric forms in vivo.
- An AT III antigen, potentially a degradation product, was also isolated.
Conclusions:
- Human serum contains AT III complexes, likely in a polymeric form.
- Further purification revealed a significant thrombin-AT III complex.
- The presence of free AT III and a distinct AT III antigen suggests ongoing AT III turnover or degradation.
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