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  • 1985-1989  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 1 (1987), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The pathogenic neisseriae, Neisseria gonorrhoeae and Neisseria meningitidis, possess an outer membrane protein, H.8, which contains a conserved monoclonal antibody (MAb)-binding epitope in all strains tested. We have cloned and sequenced a meningococcal H.8 gene, and determined the characteristics of the predicted protein. The predicted signal peptide has features characteristic of a prokaryotic lipoprotein. The region at the N-terminal end of the mature protein (39 amino acids) is primarily composed of alanine, glutamate and prollne residues arranged in imperfect repeats with the consensus sequence AAEAP. The epitope for H.8 MAb-binding was localized to a 20-amino acid sequence within this region. The remainder of the predicted amino acid sequence shows extensive homology to azurins, which are small blue copper-binding proteins found in a limited number of species of pathogenic bacteria.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We compared the structure of P.II proteins of gonococcal strain FA1090 by N-terminal sequence analysis of purified proteins and by DNA sequencing of cloned P.II genes. Regulation of P.II gene expression does not involve major DNA rearrangements, but may involve generation of frame-shifts in unexpressed P.II genes. There are probably 8 or 9 P.II genes, each possessing a common leader sequence, in the gonococcal chromosome.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 14 (1987), S. 281-287 
    ISSN: 0887-6134
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Fragment ion spectra obtained from collision-induced decomposition of protonated molecular ions have been used to determine amino acid sequences of several physalaemin-like peptides which were recently purified from rabbit stomach. This technique was chosen because the peptides were available in microgram quantities and were anticipated to contain pyroglutamate as the blocked N-terminal residue. Such spectra of several synthetic analogs of the naturally occurring peptides were obtained and analyzed to confirm the veracity of this peptide sequencing strategy. In addition, methyl ester derivatives of these synthetic peptides provided a crucial test for the spectral interpretation via the mass shifts thus induced.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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