| 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)
Pronase
|
| Index. 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 measurements |
| En ligne : |
https://drive.google.com/file/d/1cQMpUdRnNhm7Rah6-R0GtJ1Ly4TohNlV/view?usp=drive [...] |
| Format de la ressource électronique : |
Pdf |
| 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
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