Abstract
An insoluble support for affinity chromatography of carbonic anhydrase has been prepared by coupling Sulfamylon (p-aminomethylbenzene sulfonamide) to Sepharose 4B. Carbonic anhydrase binds to Sulfamylon-Sepharose very strongly and can be eluted under mild conditions by the addition of enzyme inhibitors. The gel was used to purify carbonic anhydrase from human erythrocytes and to separate isozymes B and C. It was also employed to separate native enzyme from modified carbonic anhydrases. The apoenzyme and the carboxymethyl enzyme of human carbonic anhydrase B were both isolated by this method.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 467-476 |
| Number of pages | 10 |
| Journal | Analytical Biochemistry |
| Volume | 57 |
| Issue number | 2 |
| DOIs | |
| State | Published - Feb 1974 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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Cite this
Whitney, P. L. (1974). Affinity chromatography of carbonic anhydrase. Analytical Biochemistry, 57(2), 467-476. https://doi.org/10.1016/0003-2697(74)90102-X