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Purification of tonin by affinity chromatography
Hypertension (Dallas, Tex. : 1979)
|January 1, 1981
Summary
Researchers purified rat tonin using affinity chromatography, DEAE chromatography, and gel filtration. The resulting purified tonin retained full enzymatic and immunological activity, demonstrating successful isolation.
Area of Science:
- Biochemistry
- Enzymology
Background:
- Tonin is an enzyme found in rat submaxillary glands.
- Understanding tonin's properties requires pure enzyme preparations.
Purpose of the Study:
- To purify tonin from rat submaxillary glands.
- To confirm the homogeneity and activity of the purified tonin.
Main Methods:
- Affinity chromatography using antitonin-Sepharose 4B.
- DEAE chromatography and Sephadex G-100 gel filtration.
- Enzyme homogeneity confirmed by gel filtration, electrophoresis, and immunodiffusion.
Main Results:
- Tonin was purified 11.5-fold with a 35% recovery.
- Purified tonin exhibited full enzymatic activity.
- Purified tonin demonstrated full immunological activity.
Conclusions:
- A robust purification protocol for rat tonin was established.
- The purified tonin is suitable for further biochemical and immunological studies.