Characterization of the major iron-regulated protein of Neisseria gonorrhoeae and Neissereria meningitidis
| Autor: | G. Bolen, A. Le Faou, T. A. Mietzner, Stephen A. Morse, Gary K. Schoolnik |
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| Rok vydání: | 1987 |
| Předmět: |
Molecular Sequence Data
Lysine Neisseria meningitidis Biology medicine.disease_cause Microbiology Serine chemistry.chemical_compound Bacterial Proteins Bromide Iron-Binding Proteins Spectrophotometry Mole medicine Amino Acid Sequence Amino Acids Threonine Molecular Biology Peptide sequence medicine.diagnostic_test General Medicine Neisseria gonorrhoeae Culture Media Biochemistry chemistry Periplasmic Binding Proteins Bacterial Outer Membrane Proteins |
| Zdroj: | Antonie van Leeuwenhoek. 53:465-469 |
| ISSN: | 1572-9699 0003-6072 |
| DOI: | 10.1007/bf00415504 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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