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L-4-thiazolylalanine (Protinol), a novel non-proteinogenic amino acid, demonstrates epidermal and dermal efficacy with clinically observable benefits / Gloria Portocarrero Huang in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 46, N° 1 (02/2024)
[article]
Titre : L-4-thiazolylalanine (Protinol), a novel non-proteinogenic amino acid, demonstrates epidermal and dermal efficacy with clinically observable benefits Type de document : texte imprimé Auteurs : Gloria Portocarrero Huang, Auteur ; Jolanta Idkowiak-Baldys, Auteur ; Frank Liebel, Auteur ; Constantina Jones, Auteur ; Coline Haxaire, Auteur ; Lisa DiNatale, Auteur ; Ardeshir Bayat, Auteur ; John R. Glynn, Auteur Année de publication : 2024 Article en page(s) : p. 24-38 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Acides aminés Les acides aminés (ou aminoacides) sont une classe de composés chimiques possédant deux groupes fonctionnels : à la fois un groupe carboxyle –COOH et un groupe amine –NH2. Parmi ceux-ci, les acides α-aminés se définissent par le fait que leur groupe amine est lié à l'atome de carbone adjacent au groupe acide carboxylique (le carbone α), ce qui leur confère la structure générique H2N–CHR–COOH, où R représente la chaîne latérale, qui identifie l'acide α-aminé.
Les acides α-aminés jouent un rôle fondamental en biochimie comme constituants élémentaires des protéines : ils polymérisent en formant des liaisons peptidiques qui aboutissent à de longues chaînes macromoléculaires appelées peptides.
Antiâge:Antirides
Collagène
Dermo-cosmétologie
Justification de l'allégation
Peau -- Anatomie
Peau -- PhysiologieIndex. décimale : 668.5 Parfums et cosmétiques Résumé : - Objective : Facial skin undergoes major structural and functional changes as a result of intrinsic and extrinsic factors. The goal of the current work is to demonstrate L-4-thiazolylalaine (L4, Protinol), a non-proteinogenic amino acid shown to stimulate the production of dermal proteins by fibroblasts, is an alternative efficacious topical ingredient for visible signs of ageing.
- Methods : In vitro studies using 3D human skin tissue models were performed to show changes in protein and gene expression of key dermal markers in samples treated with 0.3% L4 compared to vehicle control. In vivo evaluation of skin turnover was measured in volunteers after treatment with L4 compared to retinol. Skin biopsies (n = 30) were taken to investigate epidermal and dermal changes in cases treated with L4 and compared to retinol. Finally, a clinical evaluation (n = 28) was conducted to assess the efficacy of L4 over a base formulation using various ageing parameters within a population of women 46–66 years old with mild-to-moderate wrinkles.
- Results : In vitro studies on 3D tissues displayed significant changes in the dermal matrix via an increase in HA and pro-collagen I production and a decrease in the expression of inflammatory genes. In vivo biopsy studies demonstrated that L4 and retinol independently increased epidermal thickness and collagen remodelling significantly more compared with the base formula. Clinical evaluation showed firmer and smoother skin at day 28 post-treatment with L4 over the vehicle control without causing side effects such as redness or irritation.
- Conclusion : L4 is a novel, multi-functional ingredient which offers a superior alternative to currently available technologies for improving epidermal and dermal parameters that change during ageing and photodamage.Note de contenu : - MATERIALS AND METHODS : In vitro analysis using 3D human skin
equivalents - Gene expression from EFT400 3D tissue - Skin fluorescence measurements - In vivo treatments and histological analysis - Split-face clinical study - Firming measurements - Smoothing and wrinkle measurements - Sagging measurements - Statistical analysis
- RESULTS : L4 has pronounced effect on skin matrix components in vitro - In vivo histological analysis confirms the efficacy of L4 on epidermal and dermal components - L4 improves clinical benefits on firming, smoothing, wrinkles and sagging versus base formula after 28 daysDOI : https://doi.org/10.1111/ics.12887 En ligne : https://drive.google.com/file/d/1YZrxPHlli-4T7bMqlG6M8KHb9zQX9hMh/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=40576
in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE > Vol. 46, N° 1 (02/2024) . - p. 24-38[article]Actifs et additifs en cosmétologie / Marie-Claude Martini / Paris : Technique & Documentation - Lavoisier (1992)
Titre : Actifs et additifs en cosmétologie Type de document : texte imprimé Auteurs : Marie-Claude Martini, Editeur scientifique ; Monique Seiller, Editeur scientifique Editeur : Paris : Technique & Documentation - Lavoisier Année de publication : 1992 Autre Editeur : Cachan : Editions Médicales internationales Importance : XII-431 p. Présentation : ill. Format : 25 cm ISBN/ISSN/EAN : 978-2-85206-770-7 Note générale : Index - Bibliogr. Langues : Français (fre) Catégories : Antioxydants
Biocosmétiques
ChitosaneLe chitosane ou chitosan est un polyoside composé de la distribution aléatoire de D-glucosamine liée en ß-(1-4) (unité désacétylée) et de N-acétyl-D-glucosamine (unité acétylée). Il est produit par désacétylation chimique (en milieu alcalin) ou enzymatique de la chitine, le composant de l'exosquelette des arthropodes (crustacés) ou de l'endosquelette des céphalopodes (calmars...) ou encore de la paroi des champignons. Cette matière première est déminéralisée par traitement à l'acide chlorhydrique, puis déprotéinée en présence de soude ou de potasse et enfin décolorée grâce à un agent oxydant. Le degré d'acétylation (DA) est le pourcentage d'unités acétylées par rapport au nombre d'unités totales, il peut être déterminé par spectroscopie infrarouge à transformée de Fourier (IR-TF) ou par un titrage par une base forte. La frontière entre chitosane et chitine correspond à un DA de 50 % : en deçà le composé est nommé chitosane, au-delà , chitine. Le chitosane est soluble en milieu acide contrairement à la chitine qui est insoluble. Il est important de faire la distinction entre le degré d'acétylation (DA) et le degré de déacétylation (DD). L'un étant l'inverse de l'autre c'est-à -dire que du chitosane ayant un DD de 85 %, possède 15 % de groupements acétyles et 85 % de groupements amines sur ses chaînes.
Le chitosane est biodégradable et biocompatible (notamment hémocompatible). Il est également bactériostatique et fongistatique.
Le chitosane est également utilisé pour le traitement des eaux usées par filtration ainsi que dans divers domaines comme la cosmétique, la diététique et la médecine.
Collagène
Colorants
Conservateurs (chimie)
Cosmétiques -- Additifs
Elastine
Extraction (chimie)
Extraction par solvant
Gelée royale
Huiles essentielles
Huiles et graisses
Miel et constituants
Parfums
Phytocosmétiques
Pigments
Produits antisolaires
Produits hydratants
Produits naturels
Propolis
ProtéoglycanesUn protéoglycane est une glycoprotéine, combinaison d'une protéine et d'un glycosaminoglycane (GAG). L'association entre les deux types de chaîne s'effectue essentiellement dans l'appareil de Golgi, mais également au niveau du réticulum endoplasmique d'une cellule. La proportion de glucides des protéoglycanes peut atteindre 95 %. Ceux-ci se présentant sous la forme d'une ou plusieurs chaînes de glycosaminoglycanes non ramifiées. Les chaînes de sucres sont très longues mais pas ramifiées. Ils sont O-glycosylés, se lient à l'acide aminé sérine à l'extrémité OH. Les protéoglycanes peuvent être soit transportés à l'extérieur de la cellule par exocytose (s'intégrant alors à la matrice extracellulaire sous forme de chondroïtine-sulfate, kératan-sulfate, héparan-sulfate, dermatan-sulfate, etc.), soit entrer dans la constitution de la membrane plasmique ou du glycocalyx, jouant alors un rôle dans les relations cellule-matrice.
Les PG (protéoglycanes) ont des compositions et poids moléculaire très variés et sont hétérogènes au niveau de leur structure et de leur fonction.
Les protéoglycanes sont des composants essentiels de la matrice extracellulaire. Ce sont des pièges à eau qui sont importants pour les propriétés mécaniques des tissus cartilagineux par exemple. Les héparan sulfates peuvent avoir un rôle dans la signalisation : ce sont des co-récepteurs pour les FGF (Fibroblast Growth Factor). Les protéoglycanes jouent aussi un rôle dans la diffusion des molécules de signalisation (Wnt, Shh), ou bien en interagissant avec des inhibiteurs (Noggin). (Wikipedia)Index. décimale : 668.5 Parfums et cosmétiques Résumé : Cet ouvrage traite d'actifs et d'additifs utilisés dans les produits cosmétiques.
Les actifs sont représentés par des extraits végétaux, des extraits biologiques d'origine animale, des agents hydratants, des filtres et écrans solaires. Les additifs développés sont essentiellement les conservateurs antiseptiques, les antioxydants et les colorants.
Les auteurs qui ont participé à cet ouvrage sont tous des spécialistes du sujet qu'ils ont traité. Ils ont donc pu fournir des précisions et des compléments généralement mal connus sur les propriétés, les incompatibilités, la stabilité, les conditions d'utilisation de chacune des substances présentées.
Les tendances actuelles de la recherche et l'évolution de ce type de matières premières sont également abordées.
Bien évidemment, les problèmes législatifs ont été évoqués pour les substances inscrites sur les listes positives de la Directive Cosmétique Européenne.
Ce livre est destiné aux laboratoires de Recherche & Développement de l'industrie cosmétique, aux formulateurs, aux enseignants et aux étudiants qu'intéresse cette discipline.Note de contenu : I. PHYTOSCOMETIQUE : 1. Monographies des principales plantes utilisées en cosmétologie - 2. Technologie de la préparation des extraits végétaux - 3. Extraits végétaux Phytocosmétiques. Identifications et dosage - 4. Les corps gras végétaux et animaux
II. BIOCOSMETIQUE : 5. Extrait placentaire - 6. Collagène - 7. L'élastine - 8. Les protéoglycanes - 9. Chitosane - 10. Matières premières produites par l'abeille
III. PRODUITS DE SYNTHESE - 11. Les filtres et écrans solaires - 12. Les produits hydratants - 13. Les anti-oxydants - 14. Les conservateurs antimicrobiens
IV. PRODUITS POUR LA COLORATION : 15. Les Matières colorantes - 16. Les Pigments du troisième type - 17. Technologie de la coloration des produits cosmétiques
V. PARFUMS : 18. procédés d'extraction des huiles essentielles - 19. Procédés d'extraction des produits naturels par solvants volatilsPermalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=30778 Titre suivantRéservation
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Code-barres Cote Support Localisation Section Disponibilité 20054 668.5 MAR Monographie Bibliothèque principale Documentaires Disponible Alabaster like skin with tannin and botanical silicon / Stefan Hettwer in SOFW JOURNAL, Vol. 143, N° 3 (03/2017)
[article]
Titre : Alabaster like skin with tannin and botanical silicon Type de document : texte imprimé Auteurs : Stefan Hettwer, Auteur ; Emina Besic Gyenge, Auteur ; Brigit Suter, Auteur ; Barbara Obermayer, Auteur Année de publication : 2017 Article en page(s) : p. 18-21 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Collagène
Peau -- Soins et hygiène
Pigmentation de la peau
Silicones -- Emploi en cosmétologie
TaninsIndex. décimale : 668.5 Parfums et cosmétiques Résumé : An even complexion is key to youthful skin appearance. While the reduction of spots and unbalanced skin tone is an obvious approach to achieve an even complexion, skin texture does contribute significantly to the skin's aspect. Here we show that the use of tannic acid combined with millet seed extract providing bioavailable silicon can level out an uneven texture by strenghtening the dermal collagen network with high significance in vivo. En ligne : https://drive.google.com/file/d/1XScXjxXPZww7g62WSjYwbQUaKm50dX6I/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=28197
in SOFW JOURNAL > Vol. 143, N° 3 (03/2017) . - p. 18-21[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 18743 - Périodique Bibliothèque principale Documentaires Disponible Anionic surfactant sulfate dodecyl sodium (SDS)-induced thermodynamics and conformational changes of collagen by ultrasensitive microcalorimetry / Jie Zhang in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 3 (Année 2021)
[article]
Titre : Anionic surfactant sulfate dodecyl sodium (SDS)-induced thermodynamics and conformational changes of collagen by ultrasensitive microcalorimetry Type de document : texte imprimé Auteurs : Jie Zhang, Auteur ; Chunhua Wang, Auteur ; Fengteng Zhang, Auteur ; Wei Lin, Auteur Année de publication : 2021 Article en page(s) : 6 p. Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Analyse conformationnelle
Calorimétrie
Collagène
Stabilité thermique
Surfactants
ThermodynamiqueIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : In this communication, sulfate dodecyl sodium (SDS)-induced thermodynamics and conformational changes of collagen were studied. We used ultrasensitive differential scanning calorimetry (US-DSC) to directly monitor the thermal transition of collagen in the presence of SDS. The results show that SDS affects the conformation and thermal stability of collagen very differently depending on its concentrations. At CSDS ≤ 0.05 mM, the enhanced thermal stability of collagen indicates the stabilizing effect by SDS. However, a further increase of SDS leads to the denaturation of collagen, verifying the well-known ability of SDS to unfold proteins. This striking difference in thermodynamics and conformational changes of collagen caused by SDS concentrations can be explained in terms of their interactions. With increasing SDS, the binding of SDS to collagen can be dominated by electrostatic interaction shifting to hydrophobic interaction, and the latter plays a key role in loosening and unfolding the triple-helix structure of collagen. The important finding in the present study is the stabilizing effect of SDS on collagen molecules at extreme low concentration. Note de contenu : - Experimental section : Materials - Sample preparation - Ultra-sensitive differential scanning calorimeter (US-DSC) measurements
- The interaction between SDS and collagen by microcalorimetryDOI : https://doi.org/10.1186/s42825-021-00063-2 En ligne : https://link.springer.com/content/pdf/10.1186/s42825-021-00063-2.pdf Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=37545
in JOURNAL OF LEATHER SCIENCE AND ENGINEERING > Vol. 3 (Année 2021) . - 6 p.[article]Anti-âge : Vu à In Cosmetics Paris / Doria Maïz in PARFUMS COSMETIQUES ACTUALITES, N° 195 (06-07/2007)
[article]
Titre : Anti-âge : Vu à In Cosmetics Paris Type de document : texte imprimé Auteurs : Doria Maïz, Auteur Année de publication : 2007 Article en page(s) : p. 56-73 Langues : Français (fre) Catégories : Antiâge:Antirides
Antioxydants
Collagène
Cosmétiques
Formulation (Génie chimique)
Peptides
Photovieillissement (dermatologie)
Salons professionnels
SirtuinesIndex. décimale : 668.5 Parfums et cosmétiques Résumé : Comme toujours, l'édition parisienne de In Cosmetics est un grand cru. 30 % de visiteurs en plus par rapport à 2006, soit 6162 (avant audit ABC), 67 % venant de nombreux pays du monde. Décidément Paris attire toujours autant l'industrie cosmétique internationale. Note de contenu : - Peptides
- Les sirtuines ciblent la longévité
- Collagène: la star des techniques anti-rides
- Nouvelle cible des actifs anti-âge: le collagène XVII
- Booster de protéines
- Tenseurs
- Fiche de formulation : Sérum fluide transparent
- Anti-oxydants et photo-viellissementEn ligne : https://drive.google.com/file/d/1tVVo980to52yGhHlJYtN75-IM9fbxAH9/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=14619
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Code-barres Cote Support Localisation Section Disponibilité 007392 - Périodique Bibliothèque principale Documentaires Disponible Application of collagen colloid from chrome shavings for innovative polycondensation adhesives / Ján Sedliacik in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVI, N° 11 (11/2011)
PermalinkApplication of nonionic gemini aliphatic polyurethane surfactant for improving the performance of vegetable tanned leather / Shuangquan Lai in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXIV, N° 11 (11/2019)
PermalinkPermalinkBehavior of fatliquored leathers in a microwave field / Ying Gong in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVII, N° 2 (02/2012)
PermalinkA benefit-sharing case on an active from the amazonian biodiversity / Daniela Azevedo in SOFW JOURNAL, Vol. 143, N° 1-2 (01-02/2017)
PermalinkBenefits of a novel collagen in skin care applications / Zhao Jianfeng in PERSONAL CARE EUROPE, Vol. 14, N° 3 (06/2020)
PermalinkBiobased films prepared from collagen solutions derived from un-tanned hides / Cheng-Kung Liu in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CX, N° 2 (02/2015)
PermalinkBletilla striata polysaccharide modified collagen fiber composite sponge with rapid hemostasis function / Xingyu Yan in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 4 (Année 2022)
PermalinkCalorimetric and kinetic analysis of thermal behaviors of chrome-tanned collagen fibers using isoconversional and multivariate non-linear regression methods / Wentao Liu in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXII, N° 12 (12/2017)
PermalinkChanges in hydrothermal stability of collagen with several catechin-metal compounds : A DSC study / Chen Hui in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 92, N° 3 (05-06/2008)
PermalinkChanges to the collagen structure using vibrational spectroscopy and chemometrics : a comparison between chemical and sulfide-free leather process / Megha Mehta in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXVI, N° 11 (11/2021)
PermalinkCharacterization of fibrillar collagen types using multi-dimensional multiphoton laser scanning microscopy / V. Lutz in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 34, N° 2 (04/2012)
PermalinkPermalinkPermalinkChimie - Tannerie. Tome 2 : Le collagène & sa structure fibrillaire. Les collagènes III, V, VI, VII / G. Bouchet / 1989
PermalinkChimie - Tannerie. Tome 3 : Aspects généraux sur la réactivité du collagène - 1 / G. Bouchet / 1989
PermalinkChimie - Tannerie. Tome 4 : Aspects généraux sur la réactivité du collagène - 2 / G. Bouchet / 1989
PermalinkChimie - Tannerie. Tome 5 : Constituants mineurs du tissu : Elastine, GAGs, PG & GP ; Collagène IV et fleur (jonction derme-épiderme) / G. Bouchet / 1989
PermalinkChimie - Tannerie. Tome 6 : Epiderme - Kératines & production épidermiques - Muscles arrecteurs - Lipides - Rupture des ponts disulfiques et des liaisons O-glycosyles par actions chimiques et/ou enzymatiques / G. Bouchet / 1989
PermalinkChitosan based antibacterial composite materials for leather industry : a review / Linlin Yuan in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 3 (Année 2021)
PermalinkCollagen and keratin colloid systems with a multifunctional effect for cosmetic and technical applications / Ján Matyasovsky in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CIX, N° 9 (09/2014)
PermalinkCollagen modification using nanotechnologies : a review / Deng-Ge Gao in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVIII, N° 10 (10/2013)
PermalinkCollagen : a not so simple protein / A. J. Bailey in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 82, N° 3 (05-06/1998)
PermalinkCollagen-PEO composite nanofibers by electrospinning / Zhao Zinzhe in CHEMICAL FIBERS INTERNATIONAL, Vol. 65, N° 1 (03/2015)
PermalinkCollagen's new age : fColI(h), a wild plant-based fragment of collagen I / Ma Neus Fullana in SOFW JOURNAL, Vol. 148, N° 6 (06/2022)
PermalinkCollagen D-spacing and the effect of fat liquor addition / Katie H. Sizeland in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CX, N° 3 (03/2015)
PermalinkLe collagène n'a pas fini de surprendre / Rachida Nachat-Kappes in EXPRESSION COSMETIQUE, N° 64 (07-08/2020)
PermalinkCombattre les rides : rêve ou réalité ? / Jean-Claude Le Joliff in L'ACTUALITE CHIMIQUE, N° 299 (07/2006)
PermalinkComparative 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)
PermalinkA comparative study of various collagen fibre waste as oil sorbent materials / Weining Du in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 99, N° 6 (11-12/2015)
PermalinkPermalinkConnective tissue response to fractionated thermo-ablative erbium / M. O. Bodendorf in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 32, N° 6 (12/2010)
PermalinkConséquences de la glycation in vitro sur le collagène fibreux de type I / Mickaël Meli / 2000
PermalinkContribution à l'étude des complexes Cr3+ - acide polyacrylique et du système Cr3+ - acide polyacrylique-collagène / Abdessatar Toumi / 1984
PermalinkContribution à l'étude viscométrique en solutions diluées de collagène acido-soluble d'origine bovine / Jean-Claude Ronzon / 1987
PermalinkCross-linking phosphoric acid hydrolysates of collagen with cyanidric chloride / I. Chakarska in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 92, N° 2 (03-04/2008)
PermalinkA dehydration process for ovine hide to obtain a new collagenous material / Lluis Ollé in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 98, N° 2 (03-04/2014)
PermalinkDer kollagenreport in INDUSTRIE DU CUIR (IDC), N° 2008/05 (10-11/2008)
PermalinkDesign of a prototype to produce a new collagen material by dehydration / Lluis Ollé in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 97, N° 6 (11-12/2013)
PermalinkDevelopment and characterization of genipin cross-linked gelatin based composites incorporated with vegetable-tanned collagen fiber (VCF) / Jie Liu in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXII, N° 12 (12/2017)
PermalinkDevelopment of an in vitro model of menopause using primary human dermal fibroblasts / Noëlle Remoué in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 35, N° 6 (12/2013)
PermalinkDifferences in the reaction of condensed and hydrolysable tannins with collagen / Karl Helmer Gustavson in JOURNAL OF THE SOCIETY OF LEATHER TRADES' CHEMISTS, Vol. 50, N° 12 (12/1966)
PermalinkLa diffraction des rayons X et la spectrophotométrie IR : Meilleure connaissance de la structure du collagène, afin d'améliorer la qualité du cuir / A. Huc in TECHNICUIR, N° 7 (08-09/1973)
PermalinkDissolution characteristics of protein in an ionic liquid / Xia Chunchun in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 97, N° 1 (01-02/2013)
PermalinkDynamic mechanical thermal analysis (DMTA) of leather. Part 1 : Effect of tanning agent on the glass transition temperature of collagen / S. Jeyapalina in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 91, N° 6 (11-12/2007)
PermalinkPermalinkEffect of hydrophilic or hydrophobic interactions on the self-assembly behavior and micro-morphology of a collagen mimetic peptide / Xiaomin Luo in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 3 (Année 2021)
PermalinkEffect of ionic liquids pretreatment on the extraction of collagen from calf skin / Sicong Liu in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXIV, N° 10 (10/2019)
PermalinkEffect of pH on Al/Zr-binding sites between collagen fibers in tanning process / Shan Cao in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXI, N° 7 (07/2016)
PermalinkEffect of regioisomers of hydroxystearic acids as peroxisomal proliferator-activated receptor agonists to boost the anti-ageing potential of retinoids in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 43, N° 5 (10/2021)
PermalinkEffect of sodium chloride on structure of collagen fiber network in pickling and tanning / Li Xinxin in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXI, N° 6 (06/2016)
PermalinkEffect of tanning agents on collagen structure and response to strain in leather / Katie H. Sizeland in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXI, N° 11 (11/2016)
PermalinkEffects of alkali and acid on the solubility and molecular weight of collagen hydrolysates extracted from bovine hide in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXVII, N° 10 (10/2022)
PermalinkEffects of bating, pickling and crosslinking treatments on the characteristics of fibrous networks from un-tanned hides / Cheng-Kung Liu in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVIII, N° 3 (03/2013)
PermalinkEffects of collagen fiber addition on the combustion and thermal stability of natural rubber / Weixing Xu in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 2 (Année 2020)
PermalinkEffects of polyacrylic acid on the structure of collagen fibre / Zou Xianglong in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 98, N° 4 (07-08/2014)
PermalinkEffects of pretanning processes on bovine hide collagen structure / Eleanor M. Brown in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVII, N° 1 (01/2012)
PermalinkEffects of pretanning processes on collagen structure and reactivity in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVIII, N° 1 (01/2013)
PermalinkElectron microscopy in leather research / V. Mohanaradhakrishnan in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 54, N° 6 (06/1970)
PermalinkEnzymatic balting technology for wet blue : I. Characterization of protease activities towards chrome-tanned elastin and collagen fibers / Xu Zhang in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXIII, N° 7 (07/2018)
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PermalinkEnzymatic hydrolysis of skin shavings for preparation of collagen hydrolysates with specified molecular weight distribution / Chi Yuanlong in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 96, N° 1 (01-02/2012)
PermalinkEssential role of isoelectric point of skin/leather in leather processing / Ya-Nan Wang in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 4 (Année 2022)
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PermalinkEvaluation of protective and restoring effects of a mixture of silanols on photoaging. Use of a device allowing the quantification of contractile strengths of human fibroblasts after UVA irradiation / Sophine Robin in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 34, N° 4 (08/2012)
PermalinkEverything you wanted to know about collagen models - But were too afraid to ask ! / David Rabinovitch in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVI, N° 8 (08/2011)
PermalinkPermalinkExtraction of yak hide collagen by ultrasound-assisted lactic acid-pepsin hydrolysis method and its characterisation in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 104, N° 3 (05-06/2020)
PermalinkFabrication of composite films based on chitosan and vegetable-tanned collagen fibers crosslinked with genipin / Jie Liu in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXVI, N° 10 (10/2021)
PermalinkFabrication of highly hydrophobic paper by coating with modified collagen hydrolysate / Yaohui You in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 98, N° 2 (03-04/2014)
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PermalinkFermented bioactive for versatile anti-ageing / Xiaotong Yuan in GLOBAL PERSONAL CARE, Vol. 25, N° 1 (01/2024)
PermalinkFibre-forming properties of collagen and gelatin derived from bovine limed-split waste / Wei Xiangyi in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 99, N° 6 (11-12/2015)
PermalinkFixation covalente de divers enzymes sur films de collagène activés chimiquement. Propriétés comparées de l'aspartate amino transferase greffée et en solution / Raymond Coulet / 1973
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PermalinkA further investigation on collagen-Cr(III) interaction at molecular level / Weimo Han in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXI, N° 3 (03/2016)
PermalinkUne gestion intelligente du collagène dans les soins post-tatouage / Stefan Hettwer in EXPRESSION COSMETIQUE, N° Hors série (12/2016)
PermalinkGraft polymerization. IV. Further studies of the initiation step in the graft polymerization of vinyl monomers onto chrome-tanned collagen / Maryann M. Taylor in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXII (Année 1977)
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PermalinkHigh-quality collagen from a shiitake-based extract / Julia Comas in SOFW JOURNAL, Vol. 143, N° 6 (06/2017)
PermalinkHigh-strength collagen/delphinidin film incorporated with Vaccinium oxycoccus pigment for active and intelligent food packaging / Simiao Yin in COLLAGEN AND LEATHER, Vol. 5 (2023)
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PermalinkHygienic properties of leather finished with formulations containing collagen hydrolysate obtained by acid hydrolysis / Jan Zarlok in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 99, N° 6 (11-12/2015)
PermalinkImpact of typical surfactants on the collagenolytic and elastinolytic activities of proteases / Yanhong Li in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CX, N° 7 (07/2015)
PermalinkIn vivo topical application of acetyl aspartic acid increases fibrillin-1 and collagen IV deposition leading to a significant improvement of skin firmness / Johanna M. Gillbro in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 37, Suppl. 1 (10/2015)
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PermalinkInfluence of the collagen fibre bundle arrangements on the qualitative aspect of Nile Tilapia (Oreochromis niloticus) leather in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 107, N° 4 (07-08/2023)
PermalinkInfluencing the cutaneous carotenoid status and skin-physiological parameters by ingesting antioxidants in the form of curly-hale containing food supplements / J. Schleusener in SOFW JOURNAL, Vol. 144, N° 9 (09/2018)
PermalinkPermalinkInteraction mechanism of collagen peptides with four phenolic compounds in the ethanol-water solution / Xian Liu in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 3 (Année 2021)
PermalinkIntroduction of intra- and inter-molecular cross-bonds by mono and bifunctional sulphonyl chlorides in soluble collagen / M. S. Olivannan in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 60 (Année 1976)
PermalinkInvestigation of the interaction between epoxides and collagen in epoxy tanning based on BDDGE cross-linked collagen solution / Yuanzhi Zhang in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXV, N° 8 (08/2020)
PermalinkInvestigation of the solubility and dispersion degree of calf skin collagen in ionic liquids / Sicong Liu in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 1 (Année 2019)
PermalinkIsolation and characterization of phosphoric acid-soluble collagen from leather wastes of pig breed bulgarian white / I. Chakarska in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 90, N° 6 (11-12/2006)
PermalinkLeather retanning performance of carboxylated collagen fibres containing adsorbed Cr(III) / Qiang Taotao in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 102, N° 4 (07-08/2018)
PermalinkLeather solid waste : a review. A low cost adsorption material based on collagen fibre / Qiang Taotao in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 100, N° 3 (05-06/2016)
PermalinkManipulating chemical reactivity of collagen in tannery processing / David Rabinovitch in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CIV, N° 11 (11/2009)
PermalinkMasse moléculaire du collagène / Pierre Manhès / 1966
PermalinkMatrix proteins of the papillary dermis - Primary targets of intrinsic dermal aging ? / David Boudier in IFSCC MAGAZINE, Vol. 11, N° 3 (07-08/2008)
PermalinkMechanism of collagen processed with urea determined by thermal degradation analysis / Keyong Tang in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXV, N° 10 (10/2020)
PermalinkModelling the solubility of films prepared from collagen hydrolysate / Pavel Mokrejs in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 94, N° 6 (11-12/2010)
PermalinkModification of chrome-tanned leather waste hydrolysate with epichlorhydrin / F. Langmaier in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 90, N° 1 (01-02/2006)
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PermalinkModification of collagen hydrosylate be edac / Keyong Tang in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 92, N° 1 (01-02/2008)
PermalinkModified smart collagen biomaterials for pharmacy and adhesive applications / Ján Matyasovsky in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXI, N° 10 (10/2016)
PermalinkMolecular interactions between type I collagen and metal complex : from computational modelling to experimental characterisation / Xiao Shiwei in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 102, N° 4 (07-08/2018)
PermalinkA molecular level investigation of dialdehyde starch interaction with collagen for eco-friendly stabilization / Gladstone Christopher Jayakumar in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CX, N° 5 (05/2015)
PermalinkMolecular modeling approach to vegetable tanning : Preliminary results for gallotannin interactions with the collagen microfibril / Eleanor M. Brown in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVI, N° 5 (05/2011)
PermalinkN-Acetylglucosamine modulates function of the skin fibroblasts / A. Polubinska in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 35, N° 5 (10/2013)
PermalinkNatural leather protein's thermal stability at high temperature conditions : analyzed by AMBER software / Zhong Anhua in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 100, N° 5 (09-10/2016)
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PermalinkOlive leaf-derived PPAR agonist complex induces collagen IV synthesis in human skin models / George P. Majewski in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 43, N° 6 (12/2021)
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PermalinkOptimization of enzyme-assisted phenolic reactions applied to thermal stabilization of collagen using response surface methodology / Leticia Melo Dos Santos in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXI, N° 2 (02/2016)
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PermalinkPreparation and application of collagen-based waterborne polyurethane retanning agent / Li Chengtao in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 101, N° 3 (05-06/2017)
PermalinkPreparation and application of a high exhaustion chrome tanning auxiliary from limed fleshings / Hongjiao Liang in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 107, N° 3 (05-06/2023)
PermalinkPreparation and characterization of collagen grafted by styrene-butyl acrylate and its application for paper sizing / Sufeng Zhang in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CIX, N° 12 (12/2014)
PermalinkPreparation and characterization of collagen-tio2 nanocomposite improved by glutaraldehyde / Zhou Nan in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 90, N° 5 (09-10/2006)
PermalinkPreparation and characterization of modified protein retanning agent based on leather waste / Wang Xuechuan in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 100, N° 3 (05-06/2016)
PermalinkPreparation and drug-released properties of electrospun core-shell nanofibers / Guo Huiwen in CHEMICAL FIBERS INTERNATIONAL, Vol. 66, N° 4 (12/2016)
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PermalinkPreparation of oxidised polyvinyl alcohol using hydrogen peroxide and its application for collagen modification / Baohua Liu in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 103, N° 1 (01-02/2019)
PermalinkPrévention des vergetures par application topique. Un essai pratique à l'insu de patient et du médecin / J. Mallol in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 13, N° 1 (02/1991)
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PermalinkProcter memorial lecture collagen, 1891-1977 : retrospect and prospect / Alan Gordon Ward in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 62, N° 1 (01-02/1978)
PermalinkProcter memorial lecture collager, 1891-1977 : retrospect and prospect / Alan Gordon Ward in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 61 et 62 (Années 1977 et 1978)
PermalinkProgress of application and chemical modification of biomass collagen : a review / Wang Xuechuan in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 99, N° 5 (09-10/2015)
PermalinkProtective and restorative effects of a Commiphora mukul gum resin and triheptanoin preparation on the CCL-110 skin fibroblast cell line / Cheppail Ramachandran in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 34, N° 2 (04/2012)
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PermalinkRaw skin wastes - Used to prepare a collagen fibre adsorbent for the chromatographic separation of flavonoids / Zhang Qixian in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 98, N° 3 (05-06/2014)
PermalinkRaw skin wastes - used to prepare a flocculant for the treatment of black liquor for papermaking / Chi Yuanlong in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 95, N° 5 (09-10/2011)
PermalinkReaction mechanism of tetrakis hydroxymethyl phosphonium with collagen protein / Li Ya in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 90, N° 5 (09-10/2006)
PermalinkRéactivité de la fraction acido-soluble du collagène et comportement dans les mélanges eau-solvant organique / Daniel Herbage / 1970
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PermalinkRecent strategies of collagen-based biomaterials for cartilage repair : from structure cognition to function endowment / Xiaoyue Yu in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 4 (Année 2022)
PermalinkRecherches concernant la réaction de certains amino-acides du collagène avec les sels de zirconium / valeriu Nanescu in REVUE TECHNIQUE DES INDUSTRIES DU CUIR, Vol. LXIV (Année 1972)
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PermalinkRecovery of collagen from phosphonium tanned leather shavings and application as formaldehyde scavenger in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CIV, N° 9 (09/2009)
PermalinkRecovery of collagen hydrolysate from chrome leather shaving tannery waste through two-step hydrolysis using magnesium oxide and bating enzyme / Alvin Asava Sasia in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 103, N° 2 (03-04/2019)
PermalinkRecycling of raw materials (collagen protein) in the leather industry -high value added application of leather solid waste / Li Chengtao in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 101, N° 5 (09-10/2017)
PermalinkRedox proteomic evaluation of oxidative modification and recovery in a 3D reconstituted human skin tissue model exposed to UVB / J. M. Dyer in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 39, N° 2 (04/2017)
PermalinkRegenerating leather waste for flexible pressure sensing applications / Jie Lei in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 1 (Année 2019)
PermalinkRenewing skin from the heart of the dermis / Sonia Léglise in GLOBAL PERSONAL CARE, Vol. 22, N° 6 (06/2021)
PermalinkResearch on thermal stability, moisture and air permeability of natural leather based on the spatial conformation of the type 1 collagen molecule / Zhong Anhua in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 101, N° 5 (09-10/2017)
PermalinkResource utilisation of solid leather waste - Part I / Shyamoli Shaw in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 106, N° 3 (05-06/2022)
PermalinkRheological behaviour of alkali solubilized collagen from limed bovine split wastes / Chen Yihui in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 97, N° 5 (09-10/2013)
PermalinkSalt-pH effects on collagen thermal stability in pickling and curing / A. E. Russel in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 59 (Année 1975)
PermalinkSalt-pH effects on collagen thermal stability in pickling and curing / A. E. Russel in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 59, N° 1 (01-02/1975)
PermalinkSoy protein isolate reinforced yak skin collagen edible films for ultraviolet barring function / Ruirui Wang in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 103, N° 4 (07-08/2019)
PermalinkStabilized green tea polyphenols protecting skin from pollution / Marlène De Matos in SOFW JOURNAL, Vol. 143, N° 1/2 (01-02/2018)
PermalinkStrengthening natural protection against light / Sonia Léglise in PERSONAL CARE EUROPE, Vol. 14, N° 2 (04/2020)
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PermalinkStructure and properties of a novel collagen-soy protein isolate film via self-assembly : a comparative study / Ruirui Wang in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 104, N° 1 (01-02/2020)
PermalinkStudy on interaction mechanism between neutral salts and collagen by combining experiments with molecular dynamics simulation / Min Gu in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXVIII, N° 7 (07/2023)
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PermalinkStudy on the crosslinking modification of collagen-based materials by DMTMM in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXVIII, N° 5 (05/2023)
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PermalinkTailor-made biomaterials from collagenic wastes in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVI, N° 5 (05/2011)
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PermalinkThe aggregation behaviour of leather collagen Fibres during drying in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 102, N° 5 (09-10/2018)
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PermalinkThe combination between collagen polypeptide and calcium / Li Yanchun in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 90, N° 3 (05-06/2006)
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