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The techniques of agriculture and animal husbandry at Tell Humeida, a Middle Uruk Period (Late Chalcolithic) site on the middle Syrian Euphrates, were studied using stable isotopes of bone collagen of domestic and wild mammals and from cereal and ruderal plant seeds. Two archaeological campaigns in 2009 and 2011 yielded a small collection of bones, most of which were taxonomically indeterminable. The work had to be interrupted due to the political conflict. The faunal study comprised collagen peptide fingerprinting for taxonomic identification, followed by isotopic analysis. Multiple 14C dating were performed to date the infill to around 3600 cal BC. An isotopic analysis of the sparse plant remains suggested that irrigation and manuring were common practices. Sheep and equids predominated in the faunal assemblage. Sheep grazed on manured soils, and their diet could include millet or another C4 plant, of which, however, no carpological remains were found. The diet of equids differed from that of sheep but also that of other wild ungulates (cervids/gazelles). Their isotopic signatures indicated that they grazed in humid areas, near the watercourse. These finds indicated a settlement that was closely linked to the availability of water, which made it possible to grow crops in an almost desert-like area, and the rearing of sheep. [ABSTRACT FROM AUTHOR]

This review article provides a wide overview of important developments and applications of capillary electromigration methods in the area of peptide mapping of proteins in the period 1997–mid‐2022, including review articles on this topic. It deals with all major aspects of peptide mapping by capillary electromigration methods: i) precleavage sample preparation involving purification, preconcentration, denaturation, reduction and alkylation of protein(s) to be analyzed, ii) generation of peptide fragments by off‐line or on‐line enzymatic and/or chemical cleavage of protein(s), iii) postcleavage preparation of the generated peptide mixture for capillary electromigration separation, iv) separation of the complex peptide mixtures by one‐, two‐ and multidimensional capillary electromigration methods coupled with mass spectrometry detection, and v) a large application of peptide mapping for variable purposes, such as qualitative analysis of monoclonal antibodies and other protein biopharmaceuticals, monitoring of posttranslational modifications, determination of primary structure and investigation of function of proteins in biochemical and clinical research, characterization of proteins of variable origin as well as for protein and peptide identification in proteomic and peptidomic studies. [ABSTRACT FROM AUTHOR]