Use of immobilized cytochrome c as a ligand for affinity chromatography of thiosulfate dehydrogenase from Acidithiobacillus ferrooxidans.

Abstract:

:Three matrices 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 matrices 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 Silasorb-amine with carbodiimide activation and cytochrome c immobilized on crosslinked triazine were suitable for purification of thiosulfate dehydrogenase from Acidithiobacillus ferrooxidans. The yield with all matrices was about 90%. The purification factor of the above matrices was about 15. A new matrix based on TAT with cytochrome c represented a suitable way for thiosulfate dehydrogenase purification.

journal_name

J Biotechnol

journal_title

Journal of biotechnology

authors

Janiczek O,Pokorna B,Zemanova J,Mandl M

doi

10.1016/j.jbiotec.2005.01.014

subject

Has Abstract

pub_date

2005-05-25 00:00:00

pages

293-8

issue

3

eissn

0168-1656

issn

1873-4863

pii

S0168-1656(05)00059-3

journal_volume

117

pub_type

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