10 research outputs found

    North American Forest Grouse Harvest Regulations

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    This bulletin reviews North American forest grouse harvest regulations. Forest grouse are a highly sought-after wildlife resource across North America, both for their intrinsic value and as game species. Their unique breeding displays and the habitat they rely on are part of North America’s incredible natural heritage. Most forested landscapes in the upper latitudes of North America have the potential to provide habitat for one or more forest grouse species. This includes a large variety of vegetation types including the aspen forests of the upper Midwest, the coniferous boreal forest of Canada, the Pacific coastal rain forests that extend from Alaska to California, the Intermountain Rockies as far north as the Yukon and as far south as New Mexico and Arizona, and the mixed forests of the southern Appalachians. Across nearly the entire distribution of these forest grouse species, states and provinces have regulated harvest. Eastern states and provinces generally have shorter seasons and non-aggregated bag limits compared to western states and provinces, which tend to have more liberal season lengths, earlier start dates, and most often have aggregated bag limits for multiple forest grouse species. North American forest grouse species have different life-history strategies and yet, in many cases, harvest regulations are combined. Thus, harvest management strategies for forest grouse, especially for western states and provinces, may warrant increased evaluation to ensure appropriate harvest management and conservation of these species into the future

    Monitoring Insulin Aggregation via Capillary Electrophoresis

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    Early stages of insulin aggregation, which involve the transient formation of oligomeric aggregates, are an important aspect in the progression of Type II diabetes and in the quality control of pharmaceutical insulin production. This study is the first to utilize capillary electrophoresis (CE) with ultraviolet (UV) detection to monitor insulin oligomer formation at pH 8.0 and physiological ionic strength. The lag time to formation of the first detected species in the aggregation process was evaluated by UV-CE and thioflavin T (ThT) binding for salt concentrations from 100 mM to 250 mM. UV-CE had a significantly shorter (5–8 h) lag time than ThT binding (15–19 h). In addition, the lag time to detection of the first aggregated species via UV-CE was unaffected by salt concentration, while a trend toward an increased lag time with increased salt concentration was observed with ThT binding. This result indicates that solution ionic strength impacts early stages of aggregation and β-sheet aggregate formation differently. To observe whether CE may be applied for the analysis of biological samples containing low insulin concentrations, the limit of detection using UV and laser induced fluorescence (LIF) detection modes was determined. The limit of detection using LIF-CE, 48.4 pM, was lower than the physiological insulin concentration, verifying the utility of this technique for monitoring biological samples. LIF-CE was subsequently used to analyze the time course for fluorescein isothiocyanate (FITC)-labeled insulin oligomer formation. This study is the first to report that the FITC label prevented incorporation of insulin into oligomers, cautioning against the use of this fluorescent label as a tag for following early stages of insulin aggregation

    Unraveling the Early Events of Amyloid-β Protein (Aβ) Aggregation: Techniques for the Determination of Aβ Aggregate Size

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    The aggregation of proteins into insoluble amyloid fibrils coincides with the onset of numerous diseases. An array of techniques is available to study the different stages of the amyloid aggregation process. Recently, emphasis has been placed upon the analysis of oligomeric amyloid species, which have been hypothesized to play a key role in disease progression. This paper reviews techniques utilized to study aggregation of the amyloid-β protein (Aβ) associated with Alzheimer’s disease. In particular, the review focuses on techniques that provide information about the size or quantity of oligomeric Aβ species formed during the early stages of aggregation, including native-PAGE, SDS-PAGE, Western blotting, capillary electrophoresis, mass spectrometry, fluorescence correlation spectroscopy, light scattering, size exclusion chromatography, centrifugation, enzyme-linked immunosorbent assay, and dot blotting
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