Comparing the impacts of sediment‐spiked cadmium on Chironomidae larvae in laboratory bioassays and field microcosms and the implications for field validation of site‐specific threshold concentrations

Author(s):  
Zhihong Liu ◽  
Chi Zhang ◽  
Zhuohang Xin ◽  
Peidong Tai ◽  
Changchun Song ◽  
...  



2018 ◽  
Vol 36 (9) ◽  
pp. 827-840 ◽  
Author(s):  
Max J Krause

The Intergovernmental Panel on Climate Change (IPCC) protocol for predicting national methane emission inventories from landfills was published 22 years ago in the 1996 Revised Guidelines. There currently exists a broad dataset to review landfill parameters and reported values and their appropriateness in use and application in a range of site-specific, regional, and national estimates. Degradable organic carbon (DOC) content was found to range from 0.0105 to 0.65 g C/g waste, with an average of 0.166 g C/g waste. The fraction of DOC that would anaerobically degrade (DOC f) was reported to range from 50–83%, whereas higher and lower values have been experimentally determined for a variety of waste components, such as wood (0–50%) and food waste (50–75%). Where field validation occurred for the methane correction factor, values were substantially lower than defaults. The fraction of methane in anaerobic landfill gas ( F) default of 50% is almost universally applied and is appropriate for cellulosic wastes. The methane generation rate constant ( k) varied widely from 0.01 to 0.51 y−1, representing half-lives from 1 to 69 years. Methane oxidation (OX) default values of 0 and 10% may be valid, but values greater than 30% have been reported for porous covers at managed sites. The IPCC protocol is a practical tool with uncertainties and limitations that must be addressed when used for purposes other than developing inventories.



Author(s):  
Richard D. Powell ◽  
James F. Hainfeld ◽  
Carol M. R. Halsey ◽  
David L. Spector ◽  
Shelley Kaurin ◽  
...  

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.



2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska

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.



2006 ◽  
Vol 37 (6) ◽  
pp. 49
Author(s):  
Bruce Jancin
Keyword(s):  


1987 ◽  
Vol 48 (C9) ◽  
pp. C9-741-C9-744 ◽  
Author(s):  
W. HABENICHT ◽  
L. A. CHEWTER ◽  
M. SANDER ◽  
K. MÜLLER-DETHLEFS ◽  
E. W. SCHLAG




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