84 research outputs found

    The Cayman Crab Fly Revisited — Phylogeny and Biology of Drosophila endobranchia

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    BACKGROUND: The majority of all known drosophilid flies feed on microbes. The wide spread of microorganisms consequently mean that drosophilids also can be found on a broad range of substrates. One of the more peculiar types of habitat is shown by three species of flies that have colonized land crabs. In spite of their intriguing lifestyle, the crab flies have remained poorly studied. Perhaps the least investigated of the three crab flies is the Cayman Island endemic Drosophila endobranchia. Apart from its life cycle very little is known about this species, including its phylogenetic position, which has remained unresolved due to a cryptic set of characteristics. PRINCIPAL FINDINGS: Based on molecular data, corroborated by a re-analysis of the morphological make up, we have resolved the phylogenetic position of D. endobranchia and show that it somewhat surprisingly belongs to the large Neotropical repleta radiation, and should be considered as an aberrant member of the canalinea species group. Furthermore we also provide additional data on the behavior of these remarkable flies. CONCLUSION: Our findings reveal that the two Caribbean crab flies are not as distantly related as first thought, as both species are members of the derived repleta radiation. That this lineage has given rise to two species with the same odd type of breeding substrate is curious and prompts the question of what aspects of their shared ancestry has made these flies suitable for a life on (and inside) land crabs. Knowledge of the phylogenetic position of D. endobranchia will allow for comparative explorations and will aid in efforts aimed at understanding processes involved in drastic host shifts and extreme specialization

    Study on the Interaction of Pyrene and Humic Acid by Fluorometry

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    [中文文摘]建立了用荧光猝灭法研究芘与腐植酸间的相互作用的方法. 本方法的优点是不经分离即可测定荧光物的结合常数.[英文文摘]A fluorescence quenching method has been developed for determination association constant of pyrene with dissolved humic acids.The technique is based upon the observation that pyrene fluorescence in aqueous solution is quenched upon association with humic acid.The great advantage of this method is that the association constant of some kinds of fluorephors in a sample can be measured without separation

    Effect of Seeds upon Hydrogen-Ion Concentration of Solutions

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    Volume: 74Start Page: 215End Page: 22

    Studies on Hydrogen Sulfide Formation in Sewage

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    Notes on Precipitation of Black Sulfur Dye Waste 1

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    Potential mechanisms involved in the absorptive transport of cadmium in isolated perfused rabbit renal proximal tubules

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    a b s t r a c t Lumen-to-cell transport, cellular accumulation, and toxicity of cadmium as ionic cadmium (Cd 2+ ) or as the l-cysteine (Cys) or d,l-homocysteine (Hcy) S-conjugate of cadmium (Cys-S-Cd-S-Cys, Hcy-S-Cd-S-Hcy) were studied in isolated, perfused rabbit proximal tubular segments. When Cd 2+ (0.73 M) or Cys-S-Cd-S-Cys (0.73 M) was perfused through the lumen of S 2 segments of the proximal tubule, no visual evidence of cellular pathological changes was detected during 30 min of study. Cd 2+ -transport was temperature-dependent and was inhibited by Fe 2+ , Zn 2+ , and elevated concentrations of Ca 2+ . Luminal uptake of Cys-S-Cd-S-Cys was also temperature-dependent and was inhibited by the amino acids lcystine and l-arginine, while stimulated by l-methionine. Neither l-aspartate, l-glutamate, the synthetic dipeptide, Gly-Sar nor Zn 2+ had any effect on the rate of Cys-S-Cd-S-Cys transport. Conclusions: When delivered to the luminal compartment, Cd 2+ appears to be capable of utilizing certain transporter(s) of Zn 2+ and some transport systems sensitive to Ca 2+ and Fe 2+ . In addition, Cys-S-Cd-S-Cys and Hcy-SCd-S-Hcy appear to be transportable substrates of one or more amino acid transporters participating in luminal absorption of the amino acid l-cystine (such as system b 0,+ ). These findings indicate that multiple mechanisms could be involved in the luminal absorption of cadmium (Cd) in proximal tubular segments depending on its form. These findings provide a focus for future studies of Cd absorption in the proximal tubule

    Amino acid transporters involved in luminal transport of mercuric conjugates of cysteine in rabbit proximal tubule.

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    ABSTRACT The primary aim of the present study was to test the hypothesis that amino acid transport systems are involved in absorptive transport of dicysteinylmercury (cysteine-Hg-cysteine). Luminal disappearance flux [J D , fmol min Ϫ1 (mm tubular length) Ϫ1 ] of inorganic mercury (Hg 2ϩ ), in the form of dicysteinylmercury, was measured in isolated perfused S 2 segments with various amino acids or amino acid analogs in the luminal compartment under one of two conditions, in the presence or absence of Na ϩ . The control perfusion fluid contained 20 M dicysteinylmercury. Replacing Na ϩ in both the bathing and perfusing solutions with N-methyl-D-glucamine reduced the J D of Hg 2ϩ by about 40%. Nine amino acids and two amino acid analogs were coperfused individually (at millimolar concentrations) with dicysteinylmercury. The amino acids and amino acid analogs that had the greatest effect on the J D of Hg 2ϩ were L-cystine, L-serine, Lhistidine, L-tryptophan, and 2-(Ϫ)-endoamino-bicycloheptane-2-carboxylic acid. The greatest reduction (76%) in the total J D of Hg 2ϩ occurred when L-cystine was coperfused with dicysteinylmercury in the presence of Na ϩ . Overall, the current findings indicate that Hg 2ϩ is transported from the lumen into proximal tubular epithelial cells via amino acid transporters that recognize dicysteinylmercury. In addition, the data indicate that multiple amino acid transporters are involved in the luminal uptake of dicysteinylmercury, including the Na ϩ -dependent low-affinity L-cystine, B 0 , and ASC systems and the Na ϩ -independent L-system. Furthermore, the transport data obtained when L-cystine was added to the luminal fluid indicate strongly that dicysteinylmercury is likely transported as a molecular homolog of L-cystine
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