Tracing site-specific isotopic signatures along a Blue TitCyanistes caeruleusfood chain

Anne Charmantier; Jacques Blondel; Philippe Perret; Mireille Harmelin-Vivien

doi:10.1111/ibi.12094

Site fidelity of slimy sculpin (Cottus cognatus): insights from stable carbon and nitrogen analysis

Canadian Journal of Fisheries and Aquatic Sciences ◽

10.1139/f04-108 ◽

2004 ◽

Vol 61 (9) ◽

pp. 1717-1722 ◽

Cited By ~ 47

Author(s):

M A Gray ◽

R A Cunjak ◽

K R Munkittrick

Keyword(s):

Environmental Impacts ◽

Site Fidelity ◽

Fish Muscle ◽

Sentinel Species ◽

Agricultural Activity ◽

Local Conditions ◽

Cottus Cognatus ◽

Site Specific ◽

Isotopic Signatures ◽

Slimy Sculpin

Concerns regarding sentinel species for assessing environmental impacts include residency, abundance, and suitability for measuring responses, if effects are to be attributable to local conditions. Stable isotope analysis was used as a tool to investigate site fidelity of slimy sculpin (Cottus cognatus) to establish residency and exposure for the sculpin. We predicted that sculpin collected from sites adjacent to agricultural activity would show higher δ15N values than those collected from sites in forested areas because of isotopic enrichment by fertilizers in the former. The predominant use of chemical fertilizer applications in the region, however, resulted in no specific enrichment of 15N in sculpin collected in the agricultural region. However, there was an incremental enrichment in the fish muscle tissue of approximately 5 in δ13C values in a downstream direction, irrespective of surrounding land use. As a result, the dual-isotope comparison was successful at demonstrating site-specific isotopic signatures across sites for 30 km of the river system. The site-specific signatures suggest that slimy sculpin are not moving considerable distances among sites and are incorporating their isotopic signatures over a narrow spatial scale. The results support the use of the slimy sculpin as a sentinel species for investigating site-specific environmental impacts.

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Site-specific 15N isotopic signatures of abiotically produced N2O

Geochimica et Cosmochimica Acta ◽

10.1016/j.gca.2014.04.037 ◽

2014 ◽

Vol 139 ◽

pp. 72-82 ◽

Cited By ~ 74

Author(s):

Jannis Heil ◽

Benjamin Wolf ◽

Nicolas Brüggemann ◽

Lukas Emmenegger ◽

Béla Tuzson ◽

...

Keyword(s):

Site Specific ◽

Isotopic Signatures

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Large-cluster and combined fluorescent and gold immunoprobes

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100166920 ◽

1996 ◽

Vol 54 ◽

pp. 892-893

Author(s):

Richard D. Powell ◽

James F. Hainfeld ◽

Carol M. R. Halsey ◽

David L. Spector ◽

Shelley Kaurin ◽

...

Keyword(s):

Metal Cluster ◽

Sulfonyl Chloride ◽

Gel Filtration ◽

Cross Linking ◽

Site Specific ◽

Fab Fragments ◽

Cluster Label ◽

Covalently Linked ◽

Texas Red ◽

Fold Excess

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.

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The challenge of detecting modifications on proteins

Essays in Biochemistry ◽

10.1042/ebc20190055 ◽

2020 ◽

Vol 64 (1) ◽

pp. 135-153 ◽

Cited By ~ 1

Author(s):

Lauren Elizabeth Smith ◽

Adelina Rogowska-Wrzesinska

Keyword(s):

Mass Spectrometry ◽

Protein Function ◽

Chemical Properties ◽

Lysine Acetylation ◽

Mass Determination ◽

Post Translational Modifications ◽

Site Specific ◽

The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

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