Biochemically and Immunologically Active Alkaline Phosphatase in Archaeologically Important Bone Samples

Weser, Ulrich; Kaup, Yoka; Etspüler, Hedwig; Kenward, Nigel; Hedges, R. E. M.

doi:10.1006/jasc.1996.0068

Cited by 8 publications

(9 citation statements)

References 20 publications

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“…A number of other proteins have been reported from archaeological bone, including haemoglobin (Ascenzi et al 1985;Smith and Wilson 1990;Tuross 1991), albumin (Lowenstein et al 1981;Cattaneo et al 1992aCattaneo et al ,b, 1999Montgelard 1992) and alkaline phosphatase (Weser et al 1996). Like DNA and lipids, these proteins will be associated with fluids and cellular components in the tissue, and their presence and persistence in bone is more difficult to predict than collagen and osteocalcin.…”

Section: The Organization Of Bonementioning

confidence: 99%

The survival of organic matter in bone: a review

et al. 2002

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Section: The Organization Of Bonementioning

confidence: 99%

The survival of organic matter in bone: a review

et al. 2002

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“…Modifications of this method, e.g. alternative extraction methods (Weser et al, 1996), did not improve the quality nor the quantity of the protein extracts.…”

Section: Protein Extractionmentioning

confidence: 89%

“…Several studies have confirmed that plasma proteins and other indigenous bone proteins besides collagen can be preserved in excavated human skeletons (Cattaneo et al, 1995;Freundorfer et al, 1995;Grupe & Turban-Just, 1996); there are even reports on the detection of enzymes with a residual activity (Weser et al, 1996). After death, the proteins diffuse from the capillary system into the bone matrix where especially glycoproteins become tightly bound to the mineral by their negatively charged groups.…”

Section: Introductionmentioning

confidence: 97%

State of preservation of polymorphic plasma proteins recovered from ancient human bones

Wiechmann

Brandt

Grupe

1999

Int. J. Osteoarchaeol.

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Protected by the mineral matrix, bone proteins are capable of surviving inhumation periods of several hundreds or thousands of years in soil. While the preservation of the bone matrix protein, collagen I, is the prerequisite for a variety of archaeometric approaches, such as radiocarbon dating and the reconstruction of palaeodiet by stable isotope analysis, little is known about both the rate and state of preservation of non‐collagenous proteins. We succeeded in the isolation, electrophoretic separation (SDS‐PAGE, IEF) and immunological detection (radial immunodiffusion, IEF immunoblotting and ELISA) of plasma proteins preserved in archaeological human bones. However, sample preparation and electrophoretic methods had to be adapted to the specific demands of these aged proteins, since they are not only degraded and fragmented but also cross‐linked to other organic components, either indigenous to the bone or to contaminants from the burial environment. Complex decomposition phenomena are responsible for the altered mode of migration of aged proteins through a gel. After isoelectric focusing, the ancient proteins mainly concentrate below pH 4.45 in the pH‐gradient. Thus, highly negatively charged protein components have a better chance of preservation in bone after death. Isoelectric focusing with subsequent immunoblotting of ancient protein samples revealed protein patterns which showed marked charge‐modifications in comparison with those of modern human plasma proteins due to protein degradation (e.g. α2‐HS‐glycoprotein and α1‐antitrypsin). Nevertheless, in combination with different immunological analyses, previous results concerning the selective enrichment of α2‐HS‐glycoprotein in bone compared with other plasma glycoproteins could be confirmed. Copyright © 1999 John Wiley & Sons, Ltd.

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“…Compared with alternative extraction protocols (e.g. Weser et al, 1996), this method leads to the highest protein yields from archaeological bone that permits several duplicate analyses from one and the same extract. However, this extract is not suitable for the application of electrophoretic separation methods in our experience, because of the high proportion of non-target molecules.…”

Section: Protein Extractionmentioning

confidence: 98%

“…Masters showed that non-collagenous proteins (NCP) had a better chance of being preserved than bone collagen due to the higher affinity of NCP for the hydroxyapatite matrix. Several NCP like albumin, transferrin, α 2 -HSglycoprotein (AHSG) and some immunoglobulins have now been successfully detected in archaeological human and animal bone specimens (Tuross, 1989(Tuross, , 1991(Tuross, , 1993Grupe & TurbanJust, 1996;Weser et al, 1996), but these studies were, in general, the by-product of investigations into collagen preservation. In other case studies, the investigation of preserved NCP has been aimed at answering questions in palaeopathology (Cattaneo et al, 1994(Cattaneo et al, , 1995, species identification (Kooyman et al, 1992;Tuross & Barnes, 1996), or aspects of evolution (Shoshani et al, 1985).…”

Section: Introductionmentioning

confidence: 97%

How reliable are immunological tools for the detection of ancient proteins in fossil bones?

Brandt

Wiechmann

Grupe

2002

Intl J of Osteoarchaeology

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100 Pre-Contact human skeletons from six different excavation sites on the Peruvian coast, which showed an excellent state of preservation both on the macro-and the microscopic level, have been investigated for the preservation of three plasma proteins (α 2 -HS-glycoprotein, albumin and α 1 -antitrypsin) by enzyme-linked immunosorbent assay. A subsample of 40 skeletons out of this skeletal series had been analysed for the state of preservation of polymorphic plasma proteins by electrophoretic methods (Brandt et al., 2000), revealing extensive alterations of the target proteins by diagenesis. The question remained, therefore, as to the reliability of common immunological tools for the unambiguous detection and quantification of non-collagenous proteins in archaeological bone. In this study, we succeeded in the immunological detection of three target proteins in the skeletal remains. However, a variety of non-specific reactions were also observed with bone extracts from non-human mammals, some collagen types, and also bacterial cells. This wide range of cross-reactions with antigens not normally tested in the course of the production of commercially available antibodies adds a cautionary note to immunological approaches towards the study of ancient proteins.

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Biochemically and Immunologically Active Alkaline Phosphatase in Archaeologically Important Bone Samples

Cited by 8 publications

References 20 publications

The survival of organic matter in bone: a review

The survival of organic matter in bone: a review

State of preservation of polymorphic plasma proteins recovered from ancient human bones

How reliable are immunological tools for the detection of ancient proteins in fossil bones?

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