Analysis of site-specific N balances in heterogeneous croplands using digital methods

AbstractIn this study, site-specific N balances were calculated for a 13.1 ha heterogeneous field. Yields and N uptake as input data for N balances were determined with data from a combine harvester, reflectance measurements from satellites and tractor-mounted sensors. The correlations between the measured grain yields and yields determined by digital methods were moderate. The calculated values for the N surpluses had a wide range within the field. Nitrogen surpluses were calculated from − 76.4 to 91.3 kg ha−1, with a mean of 24.0 kg ha−1. The use of different data sources and data collection methods had an impact on the results of N balancing. The results show the need for further optimization and improvement in the accuracy of digital methods. The factors influencing N uptake and N surplus were determined by analysing soil properties of georeferenced soil samples. Soil properties showed considerable spatial variation within the field. Soil organic carbon correlated very strongly with total nitrogen content (r = 0.97), moderately with N uptake (sensor, r = 0.60) and negatively with N surplus (satellite, r = − 0.46; sensor, r = − 0.56; harvester, r = − 0.60). Nitrate content was analysed in soil cores (0 to 9 m) taken in different yield zones, and compared with the calculated N surplus; there was a strong correlation between the measured nitrate content and calculated N surplus (r = 0.82). Site-specific N balancing can contribute to a more precise identification of the risk of nitrate losses and the development of targeted nitrate reduction strategies.

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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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