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CHARACTERIZATION OF THE MAJOR IRON-REGULATED PROTEIN OF NEISSERIA-GONORRHOEAE AND NEISSERIA-MENINGITIS ANTONIE VAN LEEUWENHOEK JOURNAL OF MICROBIOLOGY Morse, S. A., Mietzner, T. A., BOLEN, G., Lefaou, A., SCHOOLNIK, G. 1987; 53 (6): 465-469

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.

View details for Web of Science ID A1987M330400016

View details for PubMedID 3130784