Characterization of the major iron-regulated protein of Neisseria gonorrhoeae and Neisseria meningitidis.
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.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001425:Bacterial Outer Membrane Proteins / Q000032:analysis* / Q000235:genetics / Q000302:isolation & purification; D001426:Bacterial Proteins; D003470:Culture Media; D033862:Iron-Binding Proteins; D008969:Molecular Sequence Data; D009344:Neisseria gonorrhoeae / Q000032:analysis* / Q000235:genetics; D009345:Neisseria meningitidis / Q000032:analysis* / Q000235:genetics; D033902:Periplasmic Binding Proteins
D000596:Amino Acids; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D003470:Culture Media; D033862:Iron-Binding Proteins; D033902:Periplasmic Binding Proteins