Characterization of the major iron-regulated protein ofNeisseria gonorrhoeaeandNeissereria meningitidis
✍ Scribed by S. A. Morse; T. A. Mietzner; G. Bolen; A. Faou; G. Schoolnik
- Publisher
- Springer Netherlands
- Year
- 1987
- Tongue
- English
- Weight
- 220 KB
- Volume
- 53
- Category
- Article
- ISSN
- 0003-6072
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✦ Synopsis
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.