Characterization of the major iron-regulated protein of Neisseria gonorrhoeae and Neissereria meningitidis |
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Authors: | S. A. Morse T. A. Mietzner G. Bolen A. Le Faou G. Schoolnik |
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Affiliation: | (1) Center for Infectious Diseases, Sexually Transmitted Diseases Laboratory Program, Centers for Disease Control, 30333 Atlanta, GA, USA;(2) Dept. of Medical Microbiology, Stanford University, 94305 Stanford, CA, USA |
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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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