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Antihaemophilic factor (factor VIII) from human granulocytes
Haematologia
|January 1, 1977
Summary
Researchers purified factor VIII (a blood clotting protein) from human granulocytes, finding it similar to plasma-derived factor VIII. This offers potential for alternative sources of this vital protein.
Area of Science:
- Biochemistry
- Hematology
- Protein purification
Background:
- Factor VIII is essential for blood coagulation.
- Current sources of Factor VIII are primarily plasma-derived.
- Investigating alternative sources like granulocytes is crucial for therapeutic supply.
Purpose of the Study:
- To isolate and purify Factor VIII from human granulocytes.
- To characterize the properties of granulocyte-derived Factor VIII.
- To compare its characteristics with plasma-derived Anti-hemophilic Factor (AHF).
Main Methods:
- Chromatography using Sephadex G-200 and DEAE-Sephadex A-50 for isolation and purification.
- Analysis of optimal pH, thermal stability, and molecular weight.
- Polyacrylamide gel electrophoresis for protein fractionation.
Main Results:
- Factor VIII was purified 60-fold from human granulocytes.
- Optimal activity was observed at pH 7.0.
- The preparation was thermolabile with a molecular weight of approximately 214,000.
- Granulocyte-derived AHF showed nearly identical characteristics to plasma-derived AHF.
Conclusions:
- Human granulocytes are a viable source for Factor VIII purification.
- Granulocyte-derived Factor VIII exhibits properties comparable to plasma-derived AHF.
- This finding supports the potential for alternative Factor VIII production methods.