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Purification of sciatin using affinity chromatography on concanavalin A-Agarose
Journal of Neurochemistry
|July 1, 1981
Summary
Sciatin, a glycoprotein from chicken sciatic nerves, promotes skeletal muscle cell development and maintenance. This study details a more efficient method for isolating sciatin, confirming its biological activity in vitro.
Area of Science:
- Neuroscience
- Cell Biology
- Biochemistry
Background:
- Sciatin is a glycoprotein found in chicken sciatic nerves.
- It exhibits trophic effects on skeletal muscle cells in culture.
- Understanding sciatin's function requires efficient purification methods.
Purpose of the Study:
- To develop a rapid and convenient method for purifying sciatin.
- To confirm the biological activity of purified sciatin on skeletal muscle cells.
Main Methods:
- Affinity chromatography using concanavalin A-agarose.
- Ion-exchange chromatography on diethylaminoethyl cellulose.
- Assessment of purity via SDS-PAGE and rocket immunoelectrophoresis.
Main Results:
- Sciatin was purified 24-fold with >97% purity.
- Purified sciatin enhanced morphological development of skeletal muscle cells in culture.
- Sciatin increased acetylcholine receptor numbers by 261%.
Conclusions:
- A more efficient purification procedure for sciatin was established.
- Purified sciatin retains its trophic activity on skeletal muscle cells.
- This method facilitates further research into sciatin's biological roles.