FINE STRUCTURE IN FOSSIL COLLAGEN

Abstract

The electron microscope was used to study fresh rat tail, fresh cow bone, scapula of Pleistocene horse (Equus occidentalis) and bone fragment of Pleistocene wolf (Canis diris). Fossil collagen was stained with uranyl acetate and phosphotungstic acid to see if it retained the selective reactivity that develops these details in fresh collagen. A step-wise degradation of the protein could be observed in some fossils and a quantitative understanding of this process is necessary if amino acid analyses are to give reliable evidence about the initial composition of the ancient proteins.