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JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) / Union internationale des sociétés de techniciens et chimistes des industries du cuir . Vol. 76, N° 5Mention de date : 09-10/1992Paru le : 01/09/1992 |
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Ajouter le résultat dans votre panierLeather research - Where now ? / R. L. Sykes in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 76, N° 5 (09-10/1992)
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Titre : Leather research - Where now ? Type de document : texte imprimé Auteurs : R. L. Sykes, Auteur Année de publication : 1992 Article en page(s) : p. 149-156 Note générale : Bibliogr. Langues : Anglais (eng) Tags : Cuirs Peaux Recherche opérationnelle Chimie Physique Problèmes environnementaux Index. décimale : 675 Technologie du cuir et de la fourrure En ligne : https://drive.google.com/file/d/17UyAlQislNv0-0sNMrjX2RZHuctPotQW/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=8573
in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 76, N° 5 (09-10/1992) . - p. 149-156[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 006988 - Périodique Bibliothèque principale Documentaires Disponible The hydrophobic effect and its importance to collagen / M. Almela in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 76, N° 5 (09-10/1992)
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Titre : The hydrophobic effect and its importance to collagen Type de document : texte imprimé Auteurs : M. Almela, Auteur ; Fernando Maldonado, Auteur ; A. Otero, Auteur ; J. Costa-Lopez, Auteur Année de publication : 1992 Article en page(s) : p. 157-161 Note générale : Bibliogr. Langues : Anglais (eng) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : The stabilisation of the structure of proteins in general and of collagen in particular, is produced through multiple weak interactions of a non-covalent nature, similar to those which take place within the medium in which it is placed. The degree of stabilisation of the protein structure will therefore be the result of the equilibrium between the internbal interactions (within the protein) and the external ones which will take place with the components of the medium. The interactions of a hydrophobic character, that take place between non-polar regions of some molecules, have an important role in the stabilisation of the structure of the proteins. The nature of the hydrophobic effect has been the subject of numerous controversies. Apart from theoretical considerations, the importance of the hydrophobic effect in collagen has been evaluated experimentally by means of the study of the interaction with surfactants having a relatively simple and defined chemical structure. A mechanism, which takes account of the participation of forces of ionic and hydrophobic nature has been established for the total interaction process. En ligne : https://drive.google.com/file/d/1Fv0EopAaMmEyP1Sg8KO423vuiXowFyTp/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=8574
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Code-barres Cote Support Localisation Section Disponibilité 006988 - Périodique Bibliothèque principale Documentaires Disponible Heterogeneous interaction between sulpho-syntans and collagen, part 7 / Z. Vinklà rek in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 76, N° 5 (09-10/1992)
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Titre : Heterogeneous interaction between sulpho-syntans and collagen, part 7 : Polyionic network hypothesis Type de document : texte imprimé Auteurs : Z. Vinklà rek, Auteur ; Z. Korenek, Auteur ; J. Vaculik ; M. Vondruska Année de publication : 1992 Article en page(s) : p. 162-168 Note générale : Bibliogr. Langues : Anglais (eng) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : During the reaction between oligoelectrolyte and collagen, a polyelectrolyte complex of the pendent-pendent type is formed. This kind of intermolecular complex has the structure of a three dimensional polyionic network, which is only intrafibrilliary polyionic network has been discussed theoretically. The structure of collagen compounds with oligoelectrolyte on the basis of naphthalene-2-sulphonic acid condensed with formaldehyde (syntanin) has then been followed up experimentally by scanning electron microscopy (SEM) and its correspondence to theroretical assumptions has been discussed. En ligne : https://drive.google.com/file/d/11vNW7j0gitPbjrCzqBRA317n0_AL5nVx/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=8575
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Code-barres Cote Support Localisation Section Disponibilité 006988 - Périodique Bibliothèque principale Documentaires Disponible Colour changes during ageing of finished leather / H. Turner in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 76, N° 5 (09-10/1992)
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Titre : Colour changes during ageing of finished leather Type de document : texte imprimé Auteurs : H. Turner, Auteur ; D. Davighi, Auteur ; Geoffrey E. Attenburrow, Auteur Année de publication : 1992 Article en page(s) : p. 169-171 Note générale : Bibliogr. Langues : Anglais (eng) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Leather was dyed pink or beige using various dyestuff types and a range of fixing agents after whichit was base coated and either left without a topcoat or given a solvent based top coat or an aqueous based topcoat. This range of samples was then subjected to accelerated ageing and colour changes were monitored. In the case of the pink leather significant colour changes were observed. It was concluded that these changes were not due to dye migration from leather to coating as originally thought but were associated with the fatliquor used in the leathermaking process. The type of topcoat applied had a significant influence on the degree of colour change observed. En ligne : https://drive.google.com/file/d/1bbT9P465bC1m5s3mgs2r3AUI3rY1wGL9/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=8576
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Code-barres Cote Support Localisation Section Disponibilité 006988 - Périodique Bibliothèque principale Documentaires Disponible
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Code-barres | Cote | Support | Localisation | Section | Disponibilité |
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006988 | - | Périodique | Bibliothèque principale | Documentaires | Disponible |