Publication details
Use of immobilized cytochrome c as a ligand for affinity chromatography of thiosulfate dehydrogenase from Acidithiobacillus ferrooxidans
| Authors | |
|---|---|
| Year of publication | 2005 |
| Type | Article in Periodical |
| Magazine / Source | Journal of Biotechnology |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | Affinity chromatography; Acidithiobacillus; thiosulfate dehydrogenase; immobilized cytochrome c |
| Description | Three matrixes were used for immobilizing the cytochrome c: Sepharose CL-4B, Silasorb SPH amine and a laboratory-prepared new matrix based on crosslinked triazine (2,4,6-tris (aminoethylamine)-1,3,5-triazine) (TAT). Cytochrome c was immobilized on the matrixes by several procedures and the amount of incorporated cytochrome c was determined. Cytochrome c immobilized on Sepharose CL-4B with periodate activation, cytochrome c immobilized on Silasorbamine with carbodiimide activation and cytochrome c immobilized on crosslinked triazine were suitable for purification of thiosulfate dehydrogenase from Acidithiobacillus ferrooxidans. The yield with all matrixes was about 90%. The purification factor of the above matrixes was about 15. A new matrix based on TAT with cytochrome c represented a suitable way for thiosulfate dehydrogenase purification. |
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