Affinity chromatography purification of cytochrome c binding enzymes. | Zendy

Angelo Azzi | Zendy; Kurt Bill | Zendy; Clemens Broger | Zendy

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Affinity chromatography purification of cytochrome c binding enzymes.

Author(s) -

Angelo Azzi,

Kurt Bill,

Clemens Broger

Publication year - 1982

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.79.8.2447

Subject(s) - cytochrome c peroxidase , cytochrome c oxidase , affinity chromatography , biochemistry , cytochrome p450 reductase , chemistry , cytochrome c , reductase , cytochrome b , cytochrome , cytochrome c1 , peroxidase , enzyme , coenzyme q – cytochrome c reductase , mitochondrion , mitochondrial dna , gene

An efficient affinity chromatography procedure for the isolation of mitochondrial cytochrome c oxidase and reductase is described. Saccharomyces cerevisiae cytochrome c was used as a ligand, bound to a thiol-Sepharose 4B gel through cysteine-107. In this way, the site of interaction of cytochrome c with cytochrome oxidase and reductase remained unmodified and available for binding to a number of partner enzymes. The procedure is adequate for the purification of all those proteins having in common the property of binding with high affinity to cytochrome c--e.g., cytochrome c oxidase, reductase, and peroxidase, sulfite oxidase, and reaction centers of photosynthetic bacteria.

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