Possibilities of extraction and characterization of ancient plasma proteins in archaeological bones.

Due to the mineral matrix bone proteins are capable of surviving during centuries after inhumation, but cross-linking with other bone proteins as well as fragmentation and complex reactions with humic acids and microorganisms lead to considerable alterations in molecular weight and structure of these proteins. Our group concentrates on polymorphic plasma proteins which diffuse out of the capillary system into the bone matrix where they adsorb to the mineralic substrate. So far, only little is known about the degradation and alteration of these proteins in fossil bones. It has to be evaluated whether the aged proteins still contain some of the information which renders them a valuable tool for forensic questions and population genetics in recent populations. Therefore we tried by modification of already existing methods to expand plasma protein identification and subtyping into the new field of aged plasma proteins.

[Serum proteins in human skeletal remains]. / Serumproteine in menschlichem Skelettmaterial.

The analysis of non-mineralbound, non-collagenous proteins from ancient Peruvian human bones with electrophoretical methods, SDS-polyacrylamide-electrophoresis and isoelectric focusing, results in molecular weight bands on the one hand and a pH-gradient distribution on the other hand, which are perhaps connected with polymorphic serum proteins. A specific protein identification is possible with immunological methods.