Mass spectrometry studies of demetallation of haemin by recombinant horse L chain apoferritin and its mutant (E 53,56,57,60 Q) | Zendy

de Val Natalia | Zendy; Herschbach Haiko | Zendy; Potier Noëlle | Zendy; Dorsselaer Alain Van | Zendy; Crichton Robert R. | Zendy

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Mass spectrometry studies of demetallation of haemin by recombinant horse L chain apoferritin and its mutant (E 53,56,57,60 Q)

Author(s) -

de Val Natalia,

Herschbach Haiko,

Potier Noëlle,

Dorsselaer Alain Van,

Crichton Robert R.

Publication year - 2006

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2006.10.034

Subject(s) - recombinant dna , horse , mutant , chemistry , mass spectrometry , microbiology and biotechnology , chromatography , biochemistry , biology , gene , paleontology

In this paper, we report the mass spectrometry studies of L‐chain apoferritin and its mutant incubated with haemin and analysed after different times of incubation: 15 days, 2 months, 6 months, 9 months and 12 months. These studies show that the recombinant L‐chain apoferritin and its mutant are able to demetallate haemin to give a hydroxyethyl protoporphyrin IX derivative in a dimeric form [Macieira, S., Martins, B. M. and Huber, R. (2003) Oxygen‐dependent coproporphyrinogen IX oxidase from Escherichia coli : one‐step purification and biochemical characterization. FEMS. Microbiology Letters 226, 31–37].

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