Abstract
The major iron-regulated protein (MIRP) was purified, from both Neisseria gonorrhoeae and N. meningitidis by selective extraction with cetyltrimethylammonium bromide followed by ion-exchange and moleculair-seive chromatography. Solutions of the purified proteins had a characteristic pink color. The overall amino acid composition of these proteins was similar, although differences were noted in the number of serine, threonine, and lysine residues. Nevertheless, the N-terminal amino acid sequence was identical through 47 residues for both the meningococcal and gonococcal MIRP. Plasma emission spectrophotometry revealed that the meningococcal 37K protein contained ca. 1 mole Fe/mole protein.
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Morse, S.A., Mietzner, T.A., Bolen, G. et al. Characterization of the major iron-regulated protein of Neisseria gonorrhoeae and Neissereria meningitidis . Antonie van Leeuwenhoek 53, 465–469 (1987). https://doi.org/10.1007/BF00415504
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DOI: https://doi.org/10.1007/BF00415504