par Semal, Patrick;Orban, Rosine 
Référence Journal of archaeological science, 22, 4, page (463-467)
Publication Publié, 1995-07
Référence Journal of archaeological science, 22, 4, page (463-467)
Publication Publié, 1995-07
Article révisé par les pairs
| Résumé : | Type I collagen is the major protein in bones. The mineral matrix protects collagen from denaturation, thus permitting the recovery of large collagen peptides from fossil bones thousands or millions of years old. Collagen peptides are more or less denatured in fossil bones, with diagenetic alteration being the major cause of such denaturation. Classical extraction methods alter the remaining large collagen peptides by extensive solubilization. A method is described here that used shorter collagen solubilization times. Resulting collagen yields are favourably compared with classical methods. The size of the large peptide (>10 kDa) fraction improves considerably. Combined with a particular concentration step, the use of this shorter solubilization technique should be useful for collagen analyses that necessitate large peptides, as in the case of palaeoimmunology. © 1995 Academic Press. All rights reserved. |
