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Comparative analysis of the proteomic profile of cattle hides that produce loose and tight leather using in-gel tryptic digestion followed by LC-MS/MS / Catherine Maidment in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXV, N° 11 (11/2020)
[article]
Titre : Comparative analysis of the proteomic profile of cattle hides that produce loose and tight leather using in-gel tryptic digestion followed by LC-MS/MS Type de document : texte imprimé Auteurs : Catherine Maidment, Auteur ; Meekyung Ahn, Auteur ; Rafea Naffa, Auteur ; Trevor Loo, Auteur ; Gillian Norris, Auteur Année de publication : 2020 Article en page(s) : p. 399-408 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Collagène
Cuir lache
Cuirs et peaux -- Analyse
Cuirs et peaux -- Défauts
Cuirs et peaux de bovins
Extraction (chimie)
Protéines
ProtéomiqueLa protéomique désigne la science qui étudie les protéomes, c'est-à -dire l'ensemble des protéines d'une cellule, d'un organite, d'un tissu, d'un organe ou d'un organisme à un moment donné et sous des conditions données.
Dans la pratique, la protéomique s'attache à identifier de manière globale les protéines extraites d'une culture cellulaire, d'un tissu ou d'un fluide biologique, leur localisation dans les compartiments cellulaires, leurs éventuelles modifications post-traductionnelles ainsi que leur quantité.
Elle permet de quantifier les variations de leur taux d'expression en fonction du temps, de leur environnement, de leur état de développement, de leur état physiologique et pathologique, de l'espèce d'origine. Elle étudie aussi les interactions que les protéines ont avec d'autres protéines, avec l'ADN ou l'ARN, ou d'autres substances.
La protéomique fonctionnelle étudie les fonctions de chaque protéine.
La protéomique étudie enfin la structure primaire, secondaire et tertiaire des protéines. (Wikipedia)
StatistiqueIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : Looseness is a defect found in leather that reduces its quality by causing a wrinkly appearance in the finished product, resulting in a reduction in its value. Earlier studies on loose leather using microscopy and Raman spectroscopy reported a change in the collagen structure of loose leather. In this study, proteomics was used to investigate the possible molecular causes of looseness in the raw material, the first time such a study has been carried out. Proteins extracted from two regions of raw hide using two different methods were analysed; those taken from the distal axilla, an area prone to looseness, and those taken from the backbone which is less prone to looseness. Analyses using 1DE-LC-MS/MS showed that although the overall collagen concentration was similar in both areas of the hide, the distribution of the different types of collagen differed. Specifically, concentrations of type I collagen, and the collagen-associated proteoglycan decorin were lower in samples taken from the distal axilla, symptomatic of a collagen network with excess space seen for these samples using confocal microscopy. This study suggests a possible link between the molecular components of raw cattle hide and looseness and more importantly between the molecular components of skin and skin defects. There is therefore potential to develop biomarkers for looseness which will enable early preventative action. Note de contenu : - EXPERIMENTAL : chemicals - Sample preparation - Protein extraction - Protein digestion - LC-MS/MS - Protein identification - Statistical analysis - Total collagen concentration - 3D confocal microscopy
- RESULTS AND DISCUSSION : Proteomic profiles : a comparison of the extraction methods - Differences between the OSP and DA regions of raw cattle hide
- Table 1 : Proteins that are significantly down regulated in the DADOI : https://doi.org/10.34314/jalca.v115i11.4184 En ligne : https://drive.google.com/file/d/1ve1EQeASe3mqkTpkqz0ZFQG6fgEMbxns/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=34846
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CXV, N° 11 (11/2020) . - p. 399-408[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 22419 - Périodique Bibliothèque principale Documentaires Disponible Insights into the molecular composition of the skins and hides used in leather manufacture / Rafea Naffa in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXIV, N° 1 (01/2019)
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Titre : Insights into the molecular composition of the skins and hides used in leather manufacture Type de document : texte imprimé Auteurs : Rafea Naffa, Auteur ; Catherine Maidment, Auteur ; Geoff Holmes ; Gillian Norris Année de publication : 2019 Article en page(s) : p. 29-36 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Cuirs et peaux -- Analyse
Cuirs et peaux de bovins
Cuirs et peaux de chèvres
Cuirs et peaux de daims
Cuirs et peaux de moutons
Structure moléculaireIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : Increasing demand for information about the effects of the beamhouse processes on animal skins and hides led to the need to determine the differences among different animal skins and hides at molecular level which results in significant changes in their strength. This is a comprehensive study of the molecular components of four animal skins commonly used to manufacture shoes, clothing and furniture to identify common indicators of skin strength. First, the strength of each species was assessed using tear strength and the denaturation temperature. Then the concentration of the following molecular compounds: amino acids, natural collagen crosslinks and glycosaminoglycans (GAGs) were determined. Significant differences in their molecular compositions were found particularly the types and amount of the natural collagen crosslinks which are known to be essential for skin strength. We found that sheep skin contained the lowest collagen content and highest GAG concentrations compared to goat and deer skins and cow hide. To the best of our knowledge, this is the first time where the collagen crosslinks of skin and hide of different species are measured and compared. This study shows that different species have different underlying molecular composition of skins and hides resulting in strength differences. This understanding will help to modify the current leather processing protocols to produce stronger leather. Note de contenu : - EXPERIMENTAL : Chemicals & reagents - Preparation of skin samples - Skin thickness measurements - Tear strength of sheep, goat, deer skins and cow hide - Differential scanning calorimetry (DSC) of sheep, goat, deer skins and cow hide - Amino acid extraction from sheep, goat, deer skins and cow hide - Derivatization of amino acids by 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate - Separation of AQC deeivatized amino acids - Extraction and quantitation of glycosaminoglycans in skins
- RESULTS AND DISCUSSION : Tear strength of sheep, goat, deer skins and cow hide - Differential scanning calorimetry (DSC) of sheep, goat and deer skins and cow hide - Amino acid composition of sheep, goat and deer skins and cow hide - Collagen I/III ratio in sheep, goat and deer skins and and cow hide - Quantitation of glycosaminoglycans (GAGs) in sheep, goat and deer skins and cow hide - Analysis of crosslinks in sheep, goat and deer skins and cow hideEn ligne : https://drive.google.com/file/d/1EPPwJTQrMvg0M1XYcXbJjQzwk94mxEY7/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=31551
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CXIV, N° 1 (01/2019) . - p. 29-36[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 20508 - Périodique Bibliothèque principale Documentaires Disponible