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From the powder of ancient human bones (200 to 1500 years old) several proteins were isolated by saline extraction. Analysis of these components by polyacrylamide gel electrophoresis and immunoelectrophoresis gave no indication for the presence of serum proteins. Analysis of the purified saline insoluble material showed an amino acid composition similar to that of collagen and in one bone a positive reaction with a collagen radioimmunoassay. The migration of the proteins in SDS polyacrylamide gels revealed a multiple banded pattern with a high tendency to aggregate and a poor resolution in and a2 bands. After cyanogen bromide cleavage several bands of low molecular weight could be resolved, indicating the occurrence of preserved methionine residues.