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. 1994 Dec 1;304(Pt 2):493–497. doi: 10.1042/bj3040493

Structural heterogeneity of Pseudomonas aeruginosa bacterioferritin.

G R Moore 1, F H Kadir 1, F K al-Massad 1, N E Le Brun 1, A J Thomson 1, C Greenwood 1, J N Keen 1, J B Findlay 1
PMCID: PMC1137519  PMID: 7998985

Abstract

The subunit composition, amino acid sequence and haem-binding characteristics of bacterioferritin (BFR) from Pseudomonas aeruginosa have been studied. Unlike other BFRs, P. aeruginosa BFR was found to contain two subunit types, designated alpha and beta, which differed considerably in their amino acid sequences. The N-terminal 69 and 55 amino acids of the alpha and beta subunits respectively were determined. The alpha subunit differed most from other BFRs. The two subunits were present in variable proportions in different preparations. The maximum stoichiometry of haem binding was found to be sample-dependent and to be different from the previously reported one per subunit [Kadir and Moore (1990) FEBS Lett. 271, 141-143]. This previous haem-binding study was shown to have been carried out with damaged protein, which contained both normal alpha and beta subunits and shorter versions of these that appeared to have been produced by cleavage of the normal subunits. The possibility that aging processes degrade ferritins and affect their haem-binding characteristics is discussed.

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Selected References

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