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  • 1
    Electronic Resource
    Electronic Resource
    Ornithine decarboxylase in Paracoccidioides brasiliensis (1996)
    Springer
    Archives of microbiology 165 (1996), S. 311-316 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsParacoccidioides brasiliensis ; Fungal ; dimorphism ; Ornithine decarboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Ornithine decarboxylase in Paracoccidioides brasiliensis, a dimorphic human pathogenic fungus, was more active at 37° C in the yeast phase and at 30° C in the mycelial phase. In contrast to other fungal systems, yeast growth and mycelium-to-yeast transition in P. brasiliensis were accompanied by a high activity of ornithine decarboxylase at the onset of the budding process, the activity of which was inhibited by 1,4-diamino-2-butanone. The activity of ornithine decarboxylase remained at a basal level during vegetative growth of both the mycelial phase and the late stage of yeast phase, and also through the yeast-to-mycelium transition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050332
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Polyamines in growth and dimorphism ofParacoccidioides brasiliensis (1996)
    Springer
    Archives of microbiology 166 (1996), S. 411-413 
    Details
    ISSN: 1432-072X
    Keywords: Paracoccidioides brasiliensis ; Fungal dimorphism ; Polyamines
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Putrescine and spermidine were the only polyamines found inParacoccidioides brasiliensis, a dimorphic fungus pathogenic for humans. Free polyamines (putrescine〉spermidine) increased during the first 24 h of yeast growth, with a second peak at 42 h, and also during the first 12 h of mycelium-to-yeast transition (spermidine〉putrescine). Conjugated and bound polyamines were also quantified. 1,4-Diamino-2-butanone decreased free putrescine and spermidine accumulation by inhibiting the activity of ornithine decarboxylase. The increase in free polyamines corresponds to bud emergence in yeast growth and to the mycelium-to-yeast transition ofP. brasiliensis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01682988
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    News & Notes: Comparison of Fungal Ornithine Decarboxylases (1996)
    Springer
    Current microbiology 33 (1996), S. 390-392 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. We designed PCR primers by comparison of the deduced amino acid sequences of several ornithine decarboxylase (ODC) genes. They were used to amplify fragments homologous to these genes from several dimorphic fungi. These were sequenced and the deduced amino acid sequences were compared with the corresponding regions of ODCs from different sources. Fungal ODCs fell into a compact group, well separated from the ODCs of other taxa. Sequence homology among fungal enzymes corresponded to their taxonomic position. Interesting patterns of amino acid conservation in ODCs from fungi, distinct from other organisms, were detected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002849900133
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  • 4
    Electronic Resource
    Electronic Resource
    Cytosolic Neutral Proteinases of Paracoccidioides brasiliensis (1998)
    Springer
    Current microbiology 37 (1998), S. 141-143 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Cytosolic proteinases were assayed in both morphological phases of Paracoccidioides brasiliensis. Preparations from the mycelial phase were more active in vitro than those from the yeast cells. Optimal proteinase activities for both phases occurred at pH's between 6.0 and 9.0, and at 45°C. Gelatin-SDS-PAGE electrophoresis separated several bands (58–112 kDa) in mycelial preparations; a single band (70 kDa) was seen in yeast preparations. Enzymatic activities were inhibited by antipain, phenyl methyl sulfonyl fluoride (PMSF), and chymostatin, suggestive of serine proteinases. Partial inhibition of the mycelial enzymes by ethylene diamine tetraacetic acid (EDTA), 1,10-phenanthroline, and iodoacetamide, also suggested the presence of cysteine- and metallo-proteinases. The enzymatic activity increased in preparations extracted from yeast cells transforming to mycelia, and decreased in preparations obtained from the reverse process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002849900353
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Cladosporium carrionii and Hormoconis resinae (C. resinae): Cell Wall and Melanin Studies (1996)
    Springer
    Current microbiology 32 (1996), S. 11-16 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Two phaeoid strains of the fungus Cladosporium carrionii (SR3 from a xerophyte species and PP8201 from a patient), and one strain of Hormoconis resinae (Cladosporium resinae), isolated from oil-impregnated soil, were analyzed for their cell wall composition by colorimetric methods, X-ray diffraction, infrared spectroscopy, and solid-state 13C-nuclear magnetic resonance. Results suggested that the cell walls were composed mainly of hexoses (34%–47%) as β-1,3-glucan (some galactose and mannose were also present) and melanin, chitin being absent. Electron microscopic observations suggested that melanin was found not only in the cell wall but also in intracellular bodies resembling melanosomes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002849900003
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Molecular cloning and sequencing of a chitin synthase gene (CHS2) of Paracoccidioides brasiliensis (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 14 (1998), S. 181-187 
    Details
    ISSN: 0749-503X
    Keywords: Paracoccidioides brasiliensis ; chitin synthase ; dimorphic fungi ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The nucleotide sequence of a chitin synthase gene (CHS2) of the dimorphic fungal human pathogen Paracoccidioides brasiliensis has been determined. The deduced amino acid sequence of Chs2p consists of 1043 residues and is highly homologous to other class II fungal chitin synthases. Computational structural analyses suggest very high similarity to other fungal chitin synthases with a highly variable region at the cytosolic amino-terminal region which may be related to its possible zymogenic nature, and the putative catalytic region close to seven membrane-spanning regions at the carboxyl terminus. The nucleotide sequence of CHS2 and its flanking regions has been submitted to GenBank under Accession Number Y09231. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
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