Preservation of bone collagen from the late cretaceous period studied by immunological techniques and atomic force microscopy
Preservation of bone collagen from the late cretaceous period studied by immunological techniques and atomic force microscopy
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DOI：
10.1021/la047682e
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发表时间：
2005-04-12
期刊：
影响因子：
3.9
通讯作者：
Calvo, JO
中科院分区：
文献类型：
--
作者：
Avci, R;Schweitzer, MH;Calvo, JO
来自阿根廷的晚白垩世鸟类骨骼组织表现出特殊的保存。Skeleton元素保存在部分关节和悬浮在三维中粒砂岩基质，表明不寻常的围死期埋藏条件。保存延伸到微观结构和分子水平。骨组织对胶原酶消化和组织化学染色有反应。原位免疫组织化学定位鸟类胶原抗体在化石组织中的结合位点。然而，免疫组化研究不能保证分子完整性的保存。蛋白质可以保留足够的抗原性用于抗体结合，即使降解可能使其不能具有原始功能。因此，我们应用原子力显微镜来解决保留的有机结构的完整性和功能性。胶原蛋白拉脱测量不仅支持用于抗体识别的胶原蛋白保存的免疫化学证据，而且还意味着整个分子完整性的保存。在生理条件下，化石和现存骨样本之间的胶原蛋白拉脱性能没有明显的差异。
Late Cretaceous avian bone tissues from Argentina demonstrate exceptional preservation. Skeletal elements are preserved in partial articulation and suspended in three dimensions in a medium-grained sandstone matrix, indicating unusual perimortem taphonomic conditions. Preservation extends to the microstructural and molecular levels. Bone tissues respond to collagenase digestion and histochemical stains. In situ immunohistochemistry localizes binding sites for avian collagen antibodies in fossil tissues. Immunohistochemical studies do not, however, guarantee the preservation of molecular integrity. A protein may retain sufficient antigenicity for antibody binding even though degradation may render it incapable of original function. Therefore, we have applied atomic force microscopy to address the integrity and functionality of retained organic structures. Collagen pull-off measurements not only support immunochemical evidence for collagen preservation for antibody recognition but also imply preservation of the whole molecular integrity. No appreciable differences in collagen pull-off properties were measured between fossil and extant bone samples under physiological conditions.