Extraction and characterisation of non-scourable chromophores from discoloured fleece wool / Jolon M. Dyer in COLORATION TECHNOLOGY, Vol. 123, N° 1 (2007)  

[article]  inCOLORATION TECHNOLOGY > Vol. 123, N° 1 (2007) . - p. 54-58 Titre : Extraction and characterisation of non-scourable chromophores from discoloured fleece wool Type de document : texte imprimé Auteurs : Jolon M. Dyer, Auteur ; S. D. Bringans, Auteur ; G. D. Aitken, Auteur ; N. I. Joyce, Auteur ; W. G. Bryson, Auteur Année de publication : 2007 Article en page(s) : p. 54-58 Note générale : Bibliogr. Langues : Anglais (eng) Index. décimale : 667.3 Teinture et impression des tissus Résumé : The colour of scoured wool is a critical determinant of its value and quality, with the presence of significant non-scourable discoloration severely limiting its use. In order to develop effective protocols for the removal or prevention of non-scourable fleece wool discoloration, it is imperative that all significant contributing chromophores are characterised and their origin established. We describe the location, extraction and characterisation of chromophores from non-scourable yellow fleece wool. Yellow discoloration was found to be located predominantly in the cuticular region of the wool fibre. Chromophoric compounds were extracted, isolated and characterised by tandem mass spectrometry, with five phenazine derivatives identified: phenazine, 1-hydroxyphenazine, phenazine-1-carboxylic acid, pyocyanine and 1-methoxyphenazine. Phenazines are brightly coloured pigments that are characteristic secondary metabolites of the bacterial genus Pseudomonas, a known ubiquitous component of the wool fleece microflora. The results of this research represent significant progress in our knowledge of wool discoloration, providing insight into both the chemical and microbial origin of non-scourable wool yellowing. DOI : 10.1111/j.1478-4408.2006.00060.x En ligne : http://onlinelibrary.wiley.com/doi/10.1111/j.1478-4408.2006.00060.x/pdf Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=3583 [article]

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Improved two-dimensional electrophoretic mapping of Japanese human hair proteins ; application to curved and straight Japanese human hairs ; and protein identification by MALDI MS and MS/MS quadrupole time-of-flight mass spectrometry / W. G. Bryson in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 42, N° 4 (08/2020)  

[article]  inINTERNATIONAL JOURNAL OF COSMETIC SCIENCE > Vol. 42, N° 4 (08/2020) . - p. 346-358 Titre : Improved two-dimensional electrophoretic mapping of Japanese human hair proteins ; application to curved and straight Japanese human hairs ; and protein identification by MALDI MS and MS/MS quadrupole time-of-flight mass spectrometry Type de document : document électronique Auteurs : W. G. Bryson, Auteur ; A. C. McCormack, Auteur ; J. E. Plowman, Auteur ; A. J. Grosvenor, Auteur ; C. J. Murphy, Auteur ; S. Nagase, Auteur ; T. Itou, Auteur ; K. Koike, Auteur Année de publication : 2020 Article en page(s) : p. 346-358 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Bases de données Cheveux Electrophorèse kératines La kératine est une protéine, synthétisée et utilisée par de nombreux êtres vivants comme élément de structure, et également l'exemple-type de protéine fibreuse. La kératine est insoluble, et peut être retrouvée sur l'épiderme de certains animaux, notamment les mammifères, ce qui leur garantit une peau imperméable. Parfois, lors d'une friction trop importante, la kératine se développe à la surface de la peau formant une callosité. Les cellules qui produisent la kératine meurent et sont remplacées continuellement. Les morceaux de kératine qui restent emprisonnés dans les cheveux sont couramment appelés des pellicules. La molécule de kératine est hélicoïdale et fibreuse, elle s'enroule autour d'autres molécules de kératine pour former des filaments intermédiaires. Ces protéines contiennent un haut taux d'acides aminés à base de soufre, principalement la cystéine, qui forment un pont disulfure entre les molécules, conférant sa rigidité à l'ensemble. La chevelure humaine est constituée à 14 % de cystéine. Il y a deux principales formes de kératines : l'alpha-kératine, ou α-keratin, présente chez les mammifères notamment, dont l'humain, et la bêta-kératine, ou β-keratin, que l'on retrouve chez les reptiles et les oiseaux. Ces deux types de kératines ne présentent clairement pas d'homologie de séquence. Chez l'être humain, la kératine est fabriquée par les kératinocytes, cellules se trouvant dans la couche profonde de l'épiderme. Les kératinocytes absorbent la mélanine (pigment fabriqué par les mélanocytes), se colorent et ainsi cette pigmentation de l'épiderme permet de protéger les kératinocytes des rayons ultraviolets du Soleil. (Wikipedia) Protéines Spectrométrie de masse Index. décimale : 668.5 Parfums et cosmétiques Résumé : - Objectives : To evaluate improved protein extraction and two-dimensional electrophoresis (2DE) separation methods with Japanese reference human hair (JRH); to determine whether fibre curvature is related to protein composition in curly and straight Japanese women’s human hair (JHH) samples; and to identify proteins from JRH 2DE maps and expression differences between curly and straight JHH. - Methods : Hair keratin and keratin-associated proteins (KAPs) were extracted intact with dithiothreitol or tris(2-carboxyethyl) phosphine from JRH or from curved or straight JHH. Extracted proteins were isoelectric-focused on first-dimensional pH gradient gel strips, then separated by molecular weight on laboratory-made, second-dimension, large format gels. The software compared protein abundance between duplicate 2DE gels of curved and straight JHH. Thirty-eight proteins from a JRH 2DE gel were enzyme-cleaved for MALDI-TOF-MS analysis to determine peptide composition, and where possible, de novo sequencing gave peptide sequence data. An in-house human hair protein database incorporating ninety-eight annotated protein sequences assisted MS analysis. - Results : 2DE gels of tris(2-carboxyethyl) phosphine-extracted JRH improved keratin and KAP resolution and number compared to those of dithiothreitol-extracted JRH and published commercially made second-dimensional gels. Silver-stained 2DE gels of the straight or curved JHH sets were remarkably similar. Over-staining to reveal basic proteins caused poor resolution of the major acidic protein classes. Software comparisons of fifty-nine resolved proteins revealed two were significantly different in abundance between curved and straight hairs but in insufficient amounts for MS analysis. MS identified twelve proteins from a JRH CBBG-stained 2DE gel: six type II keratins, three type I keratins and three high sulphur proteins. A further eight were potential conformational isoforms and isoelectric variants of the identified proteins bringing the total to twenty identified or partially identified proteins. - Conclusion : Root-end human hair extraction with tris(2-carboxyethyl) phosphine improves protein resolution and visualizes more proteins on large format 2DE gels. The two minor protein differences between duplicate straight or curved JHH 2DE gels were unlikely to change fibre structure from straight to curved hair. MS results confirmed that multiple isoforms exist of various hair proteins. Low sequence coverage prevented distinction between members in rows of homologous protein spots of similar molecular weight. Note de contenu : - MATERIALS AND METHODS : Materials - Japanese human scalp hair samples - JHH protein extraction methods - Large format 2DE method for the separation of hair proteins from JRH and JHH - Comparative analysis of protein expression with 2DE gel software - 2DE gel analysis of curved and straight whole-fibre JHH sample sets - The contribution of the cellular components to the total fibre volume of JHH - Mass spectrometric identification of JRH and JHH 2DE-resolved proteins - RESULTS AND DISCUSSION : The contribution of cellular components to the total fibre volume of JRH - Hair protein separations on 2DE gels - Mass spectral analysis of JRH proteins DOI : https://doi.org/10.1111/ics.12621 En ligne : https://drive.google.com/file/d/1xpiPo1HnSTYk-I5vdpQ3POHVJz5r4jPy/view?usp=shari [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=35286 [article]

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