scholarly journals Scratching the surface: the use of sheepskin parchment to deter textual erasure in early modern legal deeds

2021 ◽  
Vol 9 (1) ◽  
Author(s):  
Sean Paul Doherty ◽  
Stuart Henderson ◽  
Sarah Fiddyment ◽  
Jonathan Finch ◽  
Matthew J. Collins
Keyword(s):  
Twentieth Century ◽  
Early Modern ◽  
Species Identification ◽  
Low Cost ◽  
Peptide Mass Fingerprinting ◽  
Unique Structure ◽  
Peptide Mass

AbstractHistoric legal deeds are one of the most abundant resources in British archives, but also one of the most neglected. Despite the millions that survive, we know remarkably little about their manufacture, including the species of animal on which they were written. Here we present the species identification of 645 sixteenth–twentieth century skins via peptide mass fingerprinting (ZooMS), demonstrating the preferential use of sheepskin parchment. We argue that alongside their abundance and low cost, the use of sheepskins over those of other species was motivated by the increased visibility of fraudulent text erasure and modification afforded by the unique structure of their skin.

Evaluation of proteome reference maps for cross-species identification of proteins by peptide mass fingerprinting

PROTEOMICS ◽  
2002 ◽  
Vol 2 (9) ◽  
pp. 1288-1303 ◽  
Author(s):  
Ulrike Mathesius ◽  
Nijat Imin ◽  
Hancai Chen ◽  
Michael A. Djordjevic ◽  
Jeremy J. Weinman ◽  
...  
Keyword(s):  
Species Identification ◽  
Peptide Mass Fingerprinting ◽  
Peptide Mass ◽  
Proteome Reference Maps

Species identification by peptide mass fingerprinting (PMF) in fibre products preserved by association with copper-alloy artefacts

2014 ◽  
Vol 49 ◽  
pp. 524-535 ◽  
Author(s):  
Caroline Solazzo ◽  
Penelope Walton Rogers ◽  
Leslie Weber ◽  
Harriet F. Beaubien ◽  
Julie Wilson ◽  
...  
Keyword(s):  
Species Identification ◽  
Copper Alloy ◽  
Peptide Mass Fingerprinting ◽  
Peptide Mass ◽  
Fibre Products

Proteomic Analysis of Medicinal Plant Calotropis Gigantea by insilico Peptide Mass Fingerprinting

2020 ◽  
Vol 16 ◽  
Author(s):  
Saad Ur Rehman ◽  
Muhammad Rizwan ◽  
Sajid Khan ◽  
Azhar Mehmood ◽  
Anum Munir
Keyword(s):  
Medicinal Plant ◽  
Structure Prediction ◽  
3D Structure ◽  
Peptide Mass Fingerprinting ◽  
Protein Docking ◽  
Receptor Protein ◽  
Human Leukemia ◽  
Protein Database ◽  
Calotropis Gigantea ◽  
Peptide Mass

: Medicinal plants are the basic source of medicinal compounds traditionally used for the treatment of human diseases. Calotropis gigantea a medicinal plant belonging to the family of Apocynaceae in the plant kingdom and subfamily Asclepiadaceae usually bearing multiple medicinal properties to cure a variety of diseases. Background: The Peptide Mass Fingerprinting (PMF) identifies the proteins from a reference protein database by comparing the amino acid sequence that is previously stored in a database and identified. Method: The calculation of insilico peptide masses is done through the ExPASy PeptideMass and these masses are used to identify the peptides from MASCOT online server. Anticancer probability is calculated from the iACP server, docking of active peptides is done by CABS-dock the server. Objective: The purpose of the study is to identify the peptides having anti-cancerous properties by in-silico peptide mass fingerprinting. Results : The anti-cancerous peptides are identified with the MASCOT peptide mass fingerprinting server, the identified peptides are screened and only the anti-cancer are selected. De novo peptide structure prediction is used for 3D structure prediction by PEP-FOLD 3 server. The docking results confirm strong bonding with the interacting amino acids of the receptor protein of breast cancer BRCA1 which shows the best peptide binding to the Active chain, the human leukemia protein docking with peptides shows the accurate binding. Conclusion : These peptides are stable and functional and are the best way for the treatment of cancer and many other deadly diseases.

scholarly journals The Fish Pathogen Vibrio ordalii Under Iron Deprivation Produces the Siderophore Piscibactin

2019 ◽  
Vol 7 (9) ◽  
pp. 313 ◽  
Author(s):  
Pamela Ruiz ◽  
Miguel Balado ◽  
Juan Carlos Fuentes-Monteverde ◽  
Alicia E. Toranzo ◽  
Jaime Rodríguez ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Iron Uptake ◽  
Peptide Mass Fingerprinting ◽  
Iron Limitation ◽  
Fish Pathogen ◽  
Fish Pathogens ◽  
Iron Deprivation ◽  
Peptide Mass ◽  
Photobacterium Damselae ◽  
Vibrio Ordalii

Vibrio ordalii is the causative agent of vibriosis, mainly in salmonid fishes, and its virulence mechanisms are still not completely understood. In previous works we demonstrated that V. ordalii possess several iron uptake mechanisms based on heme utilization and siderophore production. The aim of the present work was to confirm the production and utilization of piscibactin as a siderophore by V. ordalii. Using genetic analysis, identification by peptide mass fingerprinting (PMF) of iron-regulated membrane proteins and chemical identification by LC-HRMS, we were able to clearly demonstrate that V. ordalii produces piscibactin under iron limitation. The synthesis and transport of this siderophore is encoded by a chromosomal gene cluster homologous to another one described in V. anguillarum, which also encodes the synthesis of piscibactin. Using β-galactosidase assays we were able to show that two potential promoters regulated by iron control the transcription of this gene cluster in V. ordalii. Moreover, biosynthetic and transport proteins corresponding to piscibactin synthesis and uptake could be identified in membrane fractions of V. ordalii cells grown under iron limitation. The synthesis of piscibactin was previously reported in other fish pathogens like Photobacterium damselae subsp. piscicida and V. anguillarum, which highlights the importance of this siderophore as a key virulence factor in Vibrionaceae bacteria infecting poikilothermic animals.

scholarly journals Optimization of Protein Extraction Method for 2DE Proteomics of Goat’s Milk

Molecules ◽  
2020 ◽  
Vol 25 (11) ◽  
pp. 2625
Author(s):  
Muzammeer Mansor ◽  
Jameel R. Al-Obaidi ◽  
Nurain Nadiah Jaafar ◽  
Intan Hakimah Ismail ◽  
Atiqah Farah Zakaria ◽  
...  
Keyword(s):  
Extraction Method ◽  
Protein Extraction ◽  
Chloroform Solution ◽  
Milk Proteins ◽  
Peptide Mass Fingerprinting ◽  
Extraction Methods ◽  
Dairy Goats ◽  
Goat’S Milk ◽  
Peptide Mass ◽  
Goat's Milk

Two-dimensional electrophoretic (2DE)-based proteomics remains a powerful tool for allergenomic analysis of goat’s milk but requires effective extraction of proteins to accurately profile the overall causative allergens. However, there are several current issues with goat’s milk allergenomic analysis, and among these are the absence of established standardized extraction method for goat’s milk proteomes and the complexity of goat’s milk matrix that may hamper the efficacy of protein extraction. This study aimed to evaluate the efficacies of three different protein extraction methods, qualitatively and quantitatively, for the 2DE-proteomics, using milk from two commercial dairy goats in Malaysia, Saanen, and Jamnapari. Goat’s milk samples from both breeds were extracted by using three different methods: a milk dilution in urea/thiourea based buffer (Method A), a triphasic separation protocol in methanol/chloroform solution (Method B), and a dilution in sulfite-based buffer (Method C). The efficacies of the extraction methods were assessed further by performing the protein concentration assay and 1D and 2D SDS-PAGE profiling, as well as identifying proteins by MALDI-TOF/TOF MS/MS. The results showed that method A recovered the highest amount of proteins (72.68% for Saanen and 71.25% for Jamnapari) and produced the highest number of protein spots (199 ± 16.1 and 267 ± 10.6 total spots for Saanen and Jamnapari, respectively) with superior gel resolution and minimal streaking. Six milk protein spots from both breeds were identified based on the positive peptide mass fingerprinting matches with ruminant milk proteins from public databases, using the Mascot software. These results attest to the fitness of the optimized protein extraction protocol, method A, for 2DE proteomic and future allergenomic analysis of the goat’s milk.

scholarly journals Identification of two highly sialylated human tear-fluid DMBT1 isoforms: the major high-molecular-mass glycoproteins in human tears

2002 ◽  
Vol 366 (2) ◽  
pp. 511-520 ◽  
Author(s):  
Benjamin L. SCHULZ ◽  
David OXLEY ◽  
Nicolle H. PACKER ◽  
Niclas G. KARLSSON
Keyword(s):  
Molecular Mass ◽  
Peptide Mass Fingerprinting ◽  
High Molecular Mass ◽  
Tear Fluid ◽  
Protein Variant ◽  
Peptide Mass ◽  
Composite Gel ◽  
Molecular Masses ◽  
Protein Components ◽  
Sialyl Lea

Human open eye tear fluid was separated by low-percentage SDS/PAGE to detect high-molecular-mass protein components. Two bands were found with apparent molecular masses of 330 and 270kDa respectively. By peptide-mass fingerprinting after tryptic digestion, the proteins were found to be isoforms of the DMBT1 gene product, with over 30% of the predicted protein covered by the tryptic peptides. By using gradient SDS/agarose/polyacrylamide composite gel electrophoresis and staining for glycosylation, it was shown that the two isoforms were the major high-molecular-mass glycoproteins of >200kDa in human tear fluid. Western blotting showed that the proteins expressed sialyl-Lea. After the release of oligosaccharides by reductive β-elimination from protein blotted on to PVDF membrane, it was revealed by liquid chromatography-MS that the O-linked oligosaccharides were comprised mainly of highly sialylated oligosaccharides with up to 16 monosaccharide units. A majority of the oligosaccharides could be described by the formula dHex0→2NeuAc1→xHexxHexNAcx(-ol), x = 1–6, where Hex stands for hexose, dHex for deoxyhexose, HexNAc for N-acetylhexosamine and NeuAc for N-acetylneuraminate. The number of sialic acids in the formula is less than 5. Interpretation of collision-induced fragmentation tandem MS confirmed the presence of sialic acid and suggested the presence of previously undescribed structures carrying the sialyl-Lea epitopes. Small amounts of neutral and sulphated species were also present. This is the first time that O-linked oligosaccharides have been detected and described from protein variant of the DMBT1 gene.

Salvage

2015 ◽  
Vol 49 (4) ◽  
pp. 845-859
Author(s):  
EVAN CALDER WILLIAMS
Keyword(s):  
Twentieth Century ◽  
Science Fiction ◽  
Early Modern ◽  
Human Body ◽  
Insurance Law ◽  
Future Possibility ◽  
Avant Garde ◽  
Personal Risk ◽  
Critical Approaches ◽  
History Of

This essay develops a history of salvage both as particular activity and as concept, arguing that it has quietly become one of the fundamental structures of thought that shape how we envision future possibility. However, the contemporary sense of the word, which designates the recuperation or search for value in what has already been destroyed, is a recent one and represents a significant transformation from the notion of salvage in early modern European maritime and insurance law. In that earlier iteration, salvage denoted payment received for helping to avert a disaster, such as keeping the ship and its goods from sinking in the first place. Passing through the dislocation of this concept into private salvage firms, firefighting companies, military usage, avant-garde art, and onto the human body itself in the guise of “personal risk,” the essay argues that the twentieth century becomes indelibly marked by a sense of the disaster that has already occurred. The second half of the essay passes into speculative culture, including fiction, video games, and film, to suggest that the most critical approaches to salvage have often come under the sign of science fiction but that the last decade in particular has shown how recent quotidian patterns of gentrification and defused antagonism have articulated stranger shifts in the figure of salvage than any speculative imaginary can currently manage.

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