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  • 1
    Electronic Resource
    Electronic Resource
    Primary Structure of the Hydrogenosomal Malic Enzyme of Trichomonas vaginalis and Its Relationship to Homologous Enzymes (1995)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 42 (1995), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . The complete nucleotide sequence has been established for two genes (maeA and maeB) coding for different subunits of the hydrogenosomal malic enzyme [malate dehydrogenase (decarboxylating) EC 1.1.1.39] of Trichomonas vaginalis. Two further genes (maeC and maeD) of this enzyme have been partially sequenced. The complete open reading frames code for polypeptides of 567 amino acids in length. These two open reading frames are similar with less than 12 percent pairwise nucleotide differences and less than 9 percent pairwise amino acid differences. The open reading frames of the two partially sequenced genes correspond to the amino-terminal part of the polypeptides coded and are similar to the corresponding parts of the completely sequenced ones. The deduced translation products of the two complete genes differ in their calculated pI values by 1.5 pH unit. The genes code for polypeptides which contain 12 or 11 amino-terminal amino-acyl residues not present in the proteins isolated from the cell. Other hydrogenosomal enzymes also have similar amino-terminal extensions which probably play a role in organellar targeting and translocation of the newly synthesized polypeptides. A comparison of 19 related enzymes from bacteria and eukaryotes with the maeA product revealed 34–45 percent amino acid identity. Phylogenetic reconstruction based on nonconservative amino acid differences with maximum parsimony (phylogenetic analysis using parsimony, PAUP) and distance based (neighbor-joining, NJ) methods showed that the T. vaginalis enzyme is the most divergent of all eukaryotic malic enzymes, indicating its long independent evolutionary history.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1995.tb05913.x
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and Specificity of Two α-Glucosidase Isoforms of the ParasiticProtist Trichomonas vaginalis (2000)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 47 (2000), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . Two isoforms of α-glucosidase were purified from the parasitic protist Trichomonas vaginalia. Both consisted of 103 kDa subunits, but differed in pH optimum and substrate specificity. Isoform 1 had a pH optimum around 4.5 and negligible activity on glucose oligomcrs other than maltose, while isoform 2 with a pH optimum of 5.5 hydrolyzed also such substrates at considerable rates. Neither had activity on glycogen or starch. Isoform 1 had a specific activity for hydrolysis of maltose of 30 U/mg protein and isoform 2 101 U/mg protein. The Km values were 0.4 mM and 2.0 mM, respectively. Isoform 2 probably corresponds to the activity detected on the cell surface.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.2000.tb00072.x
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  • 3
    Electronic Resource
    Electronic Resource
    Trichomonas hydrogenosomes contain the NADH dehydrogenase module of mitochondrial complex I (2004)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 432 (2004), S. 618-622 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Hydrogenosomes are double-membraned ATP-producing and hydrogen-producing organelles of diverse anaerobic eukaryotes. In some versions of endosymbiotic theory they are suggested to be homologues of mitochondria, but alternative views suggest they arose from an anaerobic bacterium that was ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature03149
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of substrate formulation on the efficacy of the pea moth, Cydia nigricana, sex pheromone lures (1989)
    Springer
    Entomologia experimentalis et applicata 53 (1989), S. 125-131 
    Details
    ISSN: 1570-7458
    Keywords: (E,E)-8,10-dodecadien-1-yl acetate ; sex attractant ; rubber dispensers ; release rate ; isomerization ; field experiments ; Cydia nigricana ; pea moth
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Résumé Dans la nature, l'action de (E,E)-8,10-dodécadien-1-yl-acétate, phéromone sexuelle de C. nigricana F., est significativement modifiée par le type de caoutchouc utilisé poùr la réalisation du diffuseur. Le caoutchouc vulcanisé du soufre ou avec des accélérateurs à base de composés soufrés isomérise la phéromone sexuelle de C. nigricana plus rapidement que le caoutchouc vulcanisé avec des péroxydes organiques. Le taux d'isomérisation augmente pendant l'utilisation dans la nature et/ou pendant le stockage. Les captures moyennes de mâles dépendent avant tout de la libération de la phéromone par le diffuseur. Une étude de 2×3 facteurs organisée en carré latin (6×6) a mis en évidence une interaction hautement significative entre diffuseur et dose (P〈0,01).
    Notes: Abstract Field experiments have shown that the activity of (E,E)-8,10-dodecadien-1-yl acetate, the sex pheromone of the pea moth, Cydia nigricana (F.) (Lepidoptera, Tortricidae), is significantly affected by the type of rubber substrate used for the preparation of dispensers. Rubber substrates cured with elemental sulphur or accelerators based on organic sulphur compounds isomerized pea moth pheromone faster than rubber substrates cured by organic peroxides. The degree of isomerization increased during field use and/or storage. Average catches of males were further dependent on the release rate of pheromone from the dispenser. In a 2×3 factorial experiment arranged in 6×6 Latin square design a statistically highly significant dispenser x dose interaction was demonstrated (P〈0.01).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00187993
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  • 5
    Electronic Resource
    Electronic Resource
    Primary structure and eubacterial relationships of the pyruvate:Ferredoxin oxidoreductase of the amitochondriate eukaryoteTrichomonas vaginalis (1995)
    Springer
    Journal of molecular evolution 41 (1995), S. 388-396 
    Details
    ISSN: 1432-1432
    Keywords: Hydrogenosome ; Molecular phylogeny ; Anaerobic protist
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the eukaryotic unicellular organismTrichomonas vaginalis a key step of energy metabolism, the oxidative decarboxylation of pyruvate with the formation of acetyl-CoA, is catalyzed by the iron-sulfur protein pyruvate:ferredoxin oxidoreductase (PFO) and not by the almost-ubiquitous pyruvate dehydrogenase multienzyme complex. This enzyme is localized in the hydrogenosome, an organelle bounded by a double membrane. PFO and its closely related homolog, pyruvate: flavodoxin oxidoreductase, are enzymes found in a number of archaebacteria and eubacteria. The presence of these enzymes in eukaryotes is restricted, however, to a few amitochondriate groups. To gain more insight into the evolutionary relationships ofT. vaginalis PFO we determined the primary structure of its two genes (pfoA andpfoB). The deduced amino acid sequences showed 95% positional identity. Motifs implicated in related enzymes in liganding the Fe-S centers and thiamine pyrophosphate were well conserved. TheT. vaginalis PFOs were found to be homologous to eubacterial pyruvate: flavodoxin oxidoreductases and showed about 40% amino acid identity to these enzymes over their entire length. Lack of eubacterial PFO sequences precluded a comparison.pfoA andpfoB revealed a greater distance from related enzymes of Archaebacteria. The conceptual translation of the nucleotide sequences predicted an amino-terminal pentapeptide not present in the mature protein. This processed leader sequence was similar to but shorter than leader sequences noted in other hydrogenosomal proteins. These sequences are assumed to be involved in organellar targeting and import. The results underscore the unusual characteristics ofT. vaginalis metabolism and of their hydrogenosomes. They also suggest that in its energy metabolismT. vaginalis is closer to eubacteria than archaebacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01215186
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  • 6
    Electronic Resource
    Electronic Resource
    Primary structure and eubacterial relationships of the pyruvate:Ferredoxin oxidoreductase of the amitochondriate eukaryote Trichomonas vaginalis (1995)
    Springer
    Journal of molecular evolution 41 (1995), S. 388-396 
    Details
    ISSN: 1432-1432
    Keywords: Hydrogenosome ; Molecular phylogeny ; Anaerobic protist
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the eukaryotic unicellular organism Trichomonas vaginalis a key step of energy metabolism, the oxidative decarboxylation of pyruvate with the formation of acetyl-CoA, is catalyzed by the iron-sulfur protein pyruvate:ferredoxin oxidoreductase (PFO) and not by the almost-ubiquitous pyruvate dehydrogenase multienzyme complex. This enzyme is localized in the hydrogenosome, an organelle bounded by a double membrane. PFO and its closely related homolog, pyruvate: flavodoxin oxidoreductase, are enzymes found in a number of archaebacteria and eubacteria. The presence of these enzymes in eukaryotes is restricted, however, to a few amitochondriate groups. To gain more insight into the evolutionary relationships of T. vaginalis PFO we determined the primary structure of its two genes (pfoA and pfoB). The deduced amino acid sequences showed 95% positional identity. Motifs implicated in related enzymes in liganding the Fe-S centers and thiamine pyrophosphate were well conserved. The T. vaginalis PFOs were found to be homologous to eubacterial pyruvate: flavodoxin oxidoreductases and showed about 40% amino acid identity to these enzymes over their entire length. Lack of eubacterial PFO sequences precluded a comparison. pfoA and pfoB revealed a greater distance from related enzymes of Archaebacteria. The conceptual translation of the nucleotide sequences predicted an amino-terminal pentapeptide not present in the mature protein. This processed leader sequence was similar to but shorter than leader sequences noted in other hydrogenosomal proteins. These sequences are assumed to be involved in organellar targeting and import. The results underscore the unusual characteristics of T. vaginalis metabolism and of their hydrogenosomes. They also suggest that in its energy metabolism T. vaginalis is closer to eubacteria than archaebacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00186551
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  • 7
    Electronic Resource
    Electronic Resource
    Defense Secretion of Prorhinotermes simplex: Toxicity to Insecticide Susceptible and Resistant House Fly (1999)
    Springer
    Journal of chemical ecology 25 (1999), S. 657-662 
    Details
    ISSN: 1573-1561
    Keywords: Termites ; Isoptera ; Rhinotermitidae ; Prorhinotermes simplex ; defense secretion ; (E)-1-nitropentadecene ; toxicity ; Musca domestica ; insecticide resistance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract (E)-1-Nitropentadec-1-ene (NPE), the main component of the defense secretion of Prorhinotermes simplex soldiers, is toxic to both insecticide-susceptible (S) as well as to insecticide-resistant (R) strains of the house fly, Musca domestica. The LD50 is 11.7 μg/female fly for the S strain and 9.7 μg for the R strain. The same efficacy of NPE on R and S strains indicates a different mechanism of action compared to conventional chlorinated, organophosphorus, and pyrethroid insecticides. Termite nestmates are protected against NPE by a specific detoxification mechanism. 1-Nitropentadecane, the detoxification product of NPE is nearly nontoxic to house flies, and doses up to 160 μg/fly caused only very low mortality.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020918323678
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  • 8
    Electronic Resource
    Electronic Resource
    Rubber substrates and their influence on isomerization of conjugated dienes in pheromone dispensers (1988)
    Springer
    Journal of chemical ecology 14 (1988), S. 1347-1358 
    Details
    ISSN: 1573-1561
    Keywords: Insect pheromones ; conjugated dienes ; pheromone formulations ; rubber pheromone dispensers ; isomerization ; dispensers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Release rate and degree of isomerization of pheromones with conjugated double bonds were studied in dispensers prepared from several rubber substrates. The substrates compared were made of rubber, cured with elemental sulfur or accelerators based on organic sulfur compounds or organic peroxides. Isomerization of the double bonds occurs immediately after impregnation of the substrate, and the degree of isomerization increases during field use and/or storage. The propensity of the isomers to isomerize corresponds to their proportion in the equilibrium mixture. AnE,Z isomer is isomerized faster than theE,E isomer, and finally a near-equilibrium mixture of the four isomers is present. Minimal isomerization was found in non-sulfur-cured substrates which are the material of choice.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01020139
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  • 9
    Electronic Resource
    Electronic Resource
    A Series of Bicyclic Insect Juvenile Hormone Analogs of Czech Origin: Twenty Years of Development (1997)
    Springer
    Journal of chemical ecology 23 (1997), S. 605-628 
    Details
    ISSN: 1573-1561
    Keywords: Insect juvenile hormone analogs ; 2-(4-hydroxybenzyl)-1-cycloalkanones ; Tenebrio molitor ; Coleoptera ; Tenebrionidae ; Dysdercus cingulatus ; Pyrrhocoris apterus ; Heteroptera ; Pyrrhocoridae ; Acyrthosiphon pisum ; Phorodon humuli ; Homoptera ; Aphididae ; Locusta migratoria migratortorioides ; Orthoptera ; Acrididae ; Reticulitermes lucifugus ; Prorhinotermes simplex ; Isoptera ; Rhinotermitidae ; Blattella germanica ; Blattodea ; Blattidae ; Musca domestica ; Diptera ; Muscidae ; Daphnia magna Cladocera ; Daphnidae ; Trypanosoma cruzi ; Euglenozoa ; Trypanosomatidae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Research results are summarized from a series of insect juvenile hormone analogs derived from 2-(4-hydroxybenzyl)-1-cycloalkanones, which have been investigated at the Institute of Organic Chemistry and Biochemistry in Prague during the past 20 years. At present, practical application of several prospective structures for insect control is under investigation. Biological activity values were determined to delineate the most important subseries of compounds and the most promising insect juvenile hormone analogs selected from the subseries. Carbamates, and in particular compound 47 proved to be highly active against aphids, cockroaches, flies, and many other insect species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/B:JOEC.0000006399.07779.16
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