41 research outputs found

    The use of sewage treatment works as foraging sites by insectivorous bats

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    Sewage treatment works with percolating filter beds are known to provide profitable foraging areas for insectivorous birds due to their association with high macroinvertebrate densities. Fly larvae developing on filter beds at sewage treatment works may similarly provide a valuable resource for foraging bats. Over the last two decades, however, there has been a decline in filter beds towards a system of “activated sludge”. Insects and bat activity were surveyed at 30 sites in Scotland employing these two different types of sewage treatment in order to assess the possible implications of these changes for foraging bats. Bat activity (number of passes) recorded from broad-band bat detectors was quantified at three points within each site. The biomass of aerial insects, sampled over the same period as the detector surveys, was measured using a suction trap. The biomass of insects and activity of Pipistrellus spp. was significantly higher at filter beds than at activated sludge sites. In addition, whilst foraging activity of Pipistrellus spp. at filter beds was comparable to that of adjacent “good” foraging habitat, foraging at activated sludge sites was considerably lower. This study indicates the high potential value of an anthropogenic process to foraging bats, particularly in a landscape where their insect prey has undergone a marked decline, and suggests that the current preference for activated sludge systems is likely to reduce the value of treatment works as foraging sites for bats

    Redox Regulation and Trapping Sulphenic Acid in the Peroxide Sensitive Human Mitochondrial Branched Chain Aminotransferase

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    The human branched chain aminotransferase enzymes are key regulators of glutamate metabolism in the brain and are among a growing number of redox-sensitive proteins. Studies that use thiol-specific reagents and electrospray ionization mass spectrometry demonstrate that the mitochondrial BCAT enzyme has a redox-active CXXC center, which on oxidation forms a disulfide bond (RSSR), via a cysteine sulfenic acid intermediate. Mechanistic details of this redox regulation were revealed by the use of mass spectrometry and dimedone modification. We discovered that the thiol group at position C315 of the CXXC motif acts a redox sensor, whereas the thiol group at position C318 permits reversible regulation by forming an intrasubunit disulphide bond. Because of their roles in redox regulation and catalysis, there is a growing interest in cysteine sulphenic acids. Therefore, development of chemical tags/methods to trap these transient intermediates is of immense importance
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