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A new subfraction of routine fractionation
Revue Francaise De Transfusion Et Immuno-Hematologie
|July 1, 1980
Summary
A novel protein subfraction was isolated from plasma using DEAE-sephadex A50 chromatography. This subfraction serves as a valuable starting material for purifying key proteins like C1-inactivator and ceruloplasmin.
Area of Science:
- Biochemistry
- Protein Chemistry
- Chromatography
Background:
- Plasma fractionation is crucial for isolating therapeutic proteins.
- Existing methods may not efficiently yield specific protein subfractions.
- The prothrombin complex is a key component in plasma.
Purpose of the Study:
- To develop an improved method for isolating protein subfractions from plasma.
- To identify a new starting material for purifying specific plasma proteins.
Main Methods:
- Adsorption of the prothrombin complex from plasma or cryoconcentrate supernatant onto DEAE-sephadex A50.
- Washing the adsorbent with 0.21 M NaCl solution.
Main Results:
- A new subfraction was obtained from the first washing step.
- This subfraction is suitable for purifying C1-inactivator, N-carboxypeptidase, ceruloplasmin, and kallikrein.
Conclusions:
- The described method provides a novel and efficient subfraction from plasma.
- This subfraction simplifies and enhances the purification of multiple important proteins.