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Analysis of hydroxyproline in collagen of pigskin tissue by low pressure ion chromatography separation and conductivity detection / Hong Dai in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 89, N° 4 (07-08/2005)
[article]
Titre : Analysis of hydroxyproline in collagen of pigskin tissue by low pressure ion chromatography separation and conductivity detection Type de document : texte imprimé Auteurs : Hong Dai, Auteur ; Zongcai Zhang, Auteur ; Subo Fan, Auteur ; Zhang Xinshen, Auteur Année de publication : 2005 Article en page(s) : p. 145-148 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.
Chlorhydrique, Acide
Chromatographie
Collagène -- Analyse
Cuirs et peaux -- Analyse
Cuirs et peaux de porcs
Hydrolyse
Hydroxyproline
Séparation (technologie)Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : A simplified method has been developed to determine the hydroxyproline concentration in pigskin collagen. The sample was prepared by hydrolyzing pigskin tissue collagen for 24 hours overnight at 110°C in 6M/Lhydrochloride acid followed by determination by low pressure ion chromatography separation and conductivity detection without derivatization.
Hydroxyproline was separated and detected successfully using a 5mm x 100mm long column filled with 25μm-30μm size and 0.02 mmol/g capacity cationic exchange resin. The elution solution was 0.8mmol/L nitric acid solution and the flow rate was 0.6ml/min. The concentration of the hydroxyproline sample was calculated by the five points work curve of standard stock solution. The result shows that the concentration of hyp in the sample was 3.16 ± 0.28 mmol/L. The RSD of the method was 4.63-8.97%. The recovery percentage of hyp added to the sample was 92.5-105.5%.Note de contenu : - EXPERIMENTAL METHODS : Reagents and chemicals - Apparatus - Optimum chromatography parameters
- RESULTS AND DISCUSSION : Determination of amount of hydrochloric acid needed for amino acid hydrolysis - Sample preparation - Standard curve preparation - Determination of hydroxyproline in sample - Recovery test - Determination of accuracy
- Table 1 : Optimum chromatography parameters of amino acid analysis
- Table 2 : Relationship between concentration of hydroxyproline and peak height
- Table 3 : Concentration of hydroxyproline in samples
- Table 4 : Recovery percentage of the determination for Hyp
- Table 5 : Result of accuracy experimentEn ligne : https://drive.google.com/file/d/14NZOFmgg0hcKd7hJDWqB0iiZqROk8HAy/view?usp=share [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=39245
in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 89, N° 4 (07-08/2005) . - p. 145-148[article]Exemplaires
Code-barres Cote Support Localisation Section Disponibilité aucun exemplaire Correlation of differential thermal analysis data with the shrinkage temperature of collagen and leather / J. Naghski in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXI (Année 1966)
[article]
Titre : Correlation of differential thermal analysis data with the shrinkage temperature of collagen and leather Type de document : texte imprimé Auteurs : J. Naghski, Auteur ; A. Wisnewski, Auteur ; Edward H. Harris, Auteur ; Lee P. Witnauer, Auteur Année de publication : 1966 Article en page(s) : p. 64-74 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Analyse thermique
Collagène -- Analyse
Statistique
Température de retraitIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : Shrinkage temperture data obtained on suspended specimens of raw hide substance and a variety of commercial leathers are compared with values obtained by measuring the thermodynamic changes using differential thermal analysis. In every instance the correlation between the data of these two methods was statistically highly significant, and it is concluded that they measure the same basic phenomenon. It is suggested that the absolute values for the phase transition measured by DTA be used at the reference for the thermal behavior of collagen and its products. Use of suspended specimens offers a simplified procedure, which could be defined as a method for the measurement of shrinkage temperatures. The use of pressurized equipment permitted the extension of the temperature range to include products shrinking above the boiling point of water (100°C). Note de contenu : - Instrumentation
- Sample preparation
- Typical leather-water thermogram
- Table 1 : Data from DTA and suspension shrinkage temperature measurements
- Table 2 : Summary of statistical analysisEn ligne : https://drive.google.com/file/d/1SauL0CaRzgRUUDvVv4mq8YD0ZOlxD3f2/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=37874
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. LXI (Année 1966) . - p. 64-74[article]Exemplaires (1)
Code-barres Cote Support Localisation Section Disponibilité 008496 - Périodique Archives Documentaires Exclu du prêt Extraction, identification and free radical scavenging activities of collagen-derived peptides from yak hide / Guo Song in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 106, N° 2 (03-04/2022)
[article]
Titre : Extraction, identification and free radical scavenging activities of collagen-derived peptides from yak hide Type de document : texte imprimé Auteurs : Guo Song, Auteur ; Xiaoyan Pang, Auteur ; Qiaoe Wang, Auteur ; Wei Ding, Auteur ; Zhiwen Ding, Auteur Année de publication : 2022 Article en page(s) : p. 73-82 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.
Analyse de varianceEn statistique, l'analyse de la variance (terme souvent abrégé par le terme anglais ANOVA : ANalysis Of VAriance) est un ensemble de modèles statistiques utilisés pour vérifier si les moyennes des groupes proviennent d'une même population. Les groupes correspondent aux modalités d'une variable qualitative (p. ex. variable : traitement; modalités : programme d'entrainement sportif, suppléments alimentaires ; placebo) et les moyennes sont calculés à partir d'une variable continue (p. ex. gain musculaire).
Ce test s'applique lorsque l'on mesure une ou plusieurs variables explicatives catégorielles (appelées alors facteurs de variabilité, leurs différentes modalités étant parfois appelées "niveaux") qui ont de l'influence sur la loi d'une variable continue à expliquer. On parle d'analyse à un facteur lorsque l'analyse porte sur un modèle décrit par un seul facteur de variabilité, d'analyse à deux facteurs ou d'analyse multifactorielle sinon. (Wikipedia)
Caractérisation
Collagène -- Analyse
Cuir et peau de Yak
Enzymolyse
Extraction (chimie)
Peptides
Poids moléculaires
Radicaux libres -- IdentificationIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : In this work, yak hide was used as the raw material to prepare collagen-derived peptides (YCDP) with high free radical scavenging activities (FRSA) via enzymolysis. The enzymolysis conditions were optimised via a single-factor experiment and response surface methodology (RSM) using the FRSA as the optimisation index. The optimal enzymolysis conditions were as follows: the optimal enzyme was alkaline protease, the enzymolysis pH was 8.7, the dosage of alkaline protease was 8000U/g, the temperature was 50°C, the time was 5 hours, the concentration of substrate was 5%. The FRSAs of hydroxyl, DPPH and superoxide anion radicals of the optimally prepared YCDP could be up to 39.63%, 71.08% and 69.93%, respectively, which were higher than those of CDP prepared from cattle hide under the same conditions. Further identification analyses showed that the components of YCDP with lower molecular weight contributed more to the FRSA of YCDP. Note de contenu : - MATERIALS AND METHODS : Materials - Pre-treatment of yak hide - Optimisation for the preparation of YCDP - Purification of YCDP - Characterisation
- RESULTS AND DISCUSSION : Optimisation of enzymolysis conditions - Composition and activity features of YCDP
- Table 1 : Levels of factors chosen for response surface experiment
- Table 2 : Response surface analysis design and results
- Table 3 : ANOVA of response surface quadratic model
- Table 4 : Molecular weight and content properties of the ultrafiltration fractions
- Table 5 : Amino acid composition of YCCP and CCCPEn ligne : https://drive.google.com/file/d/1nsvB0FVDUeE9p7n-ufu1CrCDUZwadjRN/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=37486
in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 106, N° 2 (03-04/2022) . - p. 73-82[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 23351 - Périodique Bibliothèque principale Documentaires Disponible Fluorescence polarization of dye-labeled collagen : local flexibility in the nonhelical region / D. Quimby in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXX (Année 1975)
[article]
Titre : Fluorescence polarization of dye-labeled collagen : local flexibility in the nonhelical region Type de document : texte imprimé Auteurs : D. Quimby, Auteur ; Lee P. Witnauer, Auteur Année de publication : 1975 Article en page(s) : p. 510-518 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Collagène -- Analyse
Colorants
Fluorescence
Matériaux -- Coloration
Mesure
Polarisation (lumière)
PronaseIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : The fluorescent dye derivatives fluorescein isothiocyanate (FI) and 5-dimethylamino-1-naphthalene sulfonyl chloride (DNS) have been covalently bound to collagen. Fluorescence from the FI conjugate is depolarized primarily hy rotation of the dye molecule about the covalent bond joining it to the protein. DNS on the other hand binds tightly to the helical regions of collagen and fluorescence from the DNS conjugate is depolarized hy rotatory diffusional motion in the nonhelical regions of the protein. Variation in pH between 3 and 10.5 has little effect on the degree of fluorescence polarization of the DNS conjugate, indicating that the degree of flexibility in the nonhelical regions remains unchanged in this pH range. Ca2+ ion induces local flexibility in the helical regions of collagen, and removal of the nonhelical regions by pronase treatment seems to render the helical regions more susceptible to perturbation by Ca2+ ions. Note de contenu : - Materials
- Dye coupling
- Pronase treatement
- Equipment and measurementsEn ligne : https://drive.google.com/file/d/1cQMpUdRnNhm7Rah6-R0GtJ1Ly4TohNlV/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=38794
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. LXX (Année 1975) . - p. 510-518[article]Exemplaires (1)
Code-barres Cote Support Localisation Section Disponibilité 008509 - Périodique Archives Documentaires Exclu du prêt Investigation 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)
[article]
Titre : Investigation of the solubility and dispersion degree of calf skin collagen in ionic liquids Type de document : texte imprimé Auteurs : Sicong Liu, Auteur ; Qian Li, Auteur ; Li Guoying, Auteur Année de publication : 2019 Article en page(s) : 12 p. Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Bovins -- Races
Chimie analytique
Collagène
Collagène -- Analyse
Collagène -- Solubilité
Dispersions et suspensions
Liquides ioniquesIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : The dissolution of collagen in ionic liquids (ILs) was highly dependent on the polarity of ILs, which was influenced by their sorts and concentrations. Herein, the solubility and dispersion degree of collagen in two sorts of ILs, namely 1-ethyl-methylimidazolium tetrafluoroborate ([EMIM][BF4]) with low polarity and 1-ethyl-3-methylimidazolium acetate ([EMIM][Ac]) with high polarity in a concentration range from 10% to 70% at 10 °C were investigated. When 150 mg of collagen was added to 30 mg of ILs, the minimum soluble collagen concentration was 0.02 mg/mL in 70% [EMIM][BF4] with lowest polarity and the maximum was 3.57 mg/mL in 70% [EMIM][Ac] with highest polarity, which indicates that soluble collagen and insoluble collagen fibers were both present. For insoluble collagens, differential scanning calorimetry showed that the thermal-stability was weakened when increasing the ILs concentration and polarity, and the fiber arrangement was looser with a more uniform lyophilized structure, observed by atomic force microscopy and scanning electron microscopy. For soluble collagens, electrophoresis patterns and Fourier transform infrared spectroscopy showed that no polypeptide chain degradation occurred during dissolution, but the thermal denaturation temperature decreased by 0.26 °C~ 7.63 °C with the increase of ILs concentrations, measured by ultra-sensitive differential scanning calorimetry. Moreover, the aggregation of collagen molecules was reduced when ILs polarity was increased as determined by fluorescence measurements and dynamic light scattering, which resulted in an increased loose fiber arrangement observed by atomic force microscopy. If the structural integrity of collagen needs to be retained, then the ILs sorts and concentrations should be considered. Note de contenu : - EXPERIMENTAL : Materials - Processing collagen with ILs - Collagen solubility in ILs - DSC of insoluble collagen fibrils - SEM of insoluble collagen fibrils - AFM measurements of insoluble and soluble collagen - SDS–PAGE patterns of soluble collagen - FTIR of soluble collagen - Fluorescence measurements of soluble collagen - DLS measurements of soluble collagen
- RESULTS AND DISCUSSION : Solubility of collagen in ILs - Thermal analysis of insoluble collagen fibrils - SEM images of insoluble collagen fibrils - AFM images of insoluble collagen fibrils - SDS-PAGE patterns of soluble collagen - FTIR spectra analysis of soluble collagen - Thermal analysis of soluble collagen - Fluorescence analysis of soluble collagen - DLS analysis of soluble collagen - AFM images of soluble collagen
- Table 1 The concentration of soluble collagen in different ILs and concentrations
- Table 2 Thermodynamic parameters of Col and collagen samples dissolved in different concentrations of [EMIM][Ac]aDOI : https://doi.org/10.1186/s42825-019-0013-9 En ligne : https://link.springer.com/content/pdf/10.1186/s42825-019-0013-9.pdf Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=36945
in JOURNAL OF LEATHER SCIENCE AND ENGINEERING > Vol. 1 (Année 2019) . - 12 p.[article]Exemplaires
Code-barres Cote Support Localisation Section Disponibilité aucun exemplaire Link lock : an explanation of the chemical stabilisation of collagen / Anthony D. Covington in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 92, N° 1 (01-02/2008)
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PermalinkPhysiological and cell biological properties in vitro of collagen isolated from calf limed splits / G. I. Ly in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 88, N° 2 (03-04/2004)
PermalinkStructure of skin in collagenous fibres : crossbreeds from black-and-white-cows X bulls of beef breeds / Piotr Zapletal in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 85, N° 6 (11-12/2001)
PermalinkStudies on collagen structure using X-ray scattering on a closed-loop leather process / Yi Zhang in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXV, N° 10 (10/2020)
PermalinkStudy on changes of collagen fibril structure in pigskin tissue after enzyme / Wang Yingmei in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 89, N° 2 (03-04/2005)
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)
PermalinkToxicity evaluation of collagen hydrolysates from chrome shavings and their potential use in the preparation of amino acid fertilizer for crop growth / Li Zhao in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 4 (Année 2022)
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