Extraction of osteocalcin from fossil bones and teeth

Ulrich, Magda M. W.; Perizonius, W.R.K.; Spoor, C. F.; Sandberg, Philip A.; Vermeer, Cees

doi:10.1016/0006-291x(87)90426-8

Cited by 52 publications

(29 citation statements)

References 11 publications

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“…Non-collagenous proteins, including osteocalcin (Ulrich et al, 1987), albumin (Tuross, 1989) and haemoglobins (Ascenzi et al, 1985;Smith & Wilson, 1990) have also been detected in archaeological and palaeontological bone by application of immunological techniques such as immunoblotting and the enzyme-linked inhibition assay (ELISA) (for a recent review, see Childs & Pollard, 1992). The recovery of DNA from bones by use of the polymerase chain reaction raises many exciting possibilities for anthropological and palaeontological investigation (Hagelberg et al, 1989;Hedges & Sykes, 1992;Brown & Brown, 1993).…”

Section: Introductionmentioning

confidence: 97%

“…technique to date collagen-derived amino acids (Bada, 1991) scope exists for the use of this technique in connection with the minor, more robust, proteins associated with the biomineralisation process (Ulrich et al, 1987). Estimations of the nitrogen ( 15 N) and carbon ( 13 C) isotope compositions of bone collagen have been conducted for the purposes of estimating palaeodiet (Vogel & van der Merwe, 1977;DeNiro, 1987;Schwarcz, 1991).…”

Section: Introductionmentioning

confidence: 99%

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Preliminary Results for the Analysis of Lipids in Ancient Bone

Evershed

Turner‐Walker

Hedges

et al. 1995

Journal of Archaeological Science

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Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Preliminary Results for the Analysis of Lipids in Ancient Bone

Evershed

Turner‐Walker

Hedges

et al. 1995

Journal of Archaeological Science

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“…It is also important to note that these parameters primarily depend on ancient bone collagen as the levels remain largely unchanged (a high percentage of collagen is retained, as gleaned by laboratory experiments on bone taphonomy (6)). Additionally, antibody-based immunostaining methods have given indirect evidence of intact peptide amide bonds (43)(44)(45) to aid some of the first evidence of protein other than collagen and osteocalcin in ancient mammoth (43) and human specimens (46).…”

mentioning

confidence: 99%

Preserved Proteins from Extinct Bison latifrons Identified by Tandem Mass Spectrometry; Hydroxylysine Glycosides are a Common Feature of Ancient Collagen

Hill

Wither

Nemkov

et al. 2015

Molecular & Cellular Proteomics

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Bone samples from several vertebrates were collected from the Ziegler Reservoir fossil site, in Snowmass Village, Colorado, and processed for proteomics analysis. The specimens come from Pleistocene megafauna Bison latifrons, dating back ϳ120,000 years. Proteomics analysis using a simplified sample preparation procedure and tandem mass spectrometry (MS/MS) was applied to obtain protein identifications. Several bioinformatics resources were used to obtain peptide identifications based on sequence homology to extant species with annotated genomes. With the exception of soil sample controls, all samples resulted in confident peptide identifications that mapped to type I collagen. In addition, we analyzed a specimen from the extinct B. latifrons that yielded peptide identifications mapping to over 33 bovine proteins. Our analysis resulted in extensive fibrillar collagen sequence coverage, including the identification of posttranslational modifications. Hydroxylysine glucosylgalactosylation, a modification thought to be involved in collagen fiber formation and bone mineralization, was identified for the first time in an ancient protein dataset. Meta-analysis of data from other studies indicates that this modification may be common in well-preserved prehistoric samples. Additional peptide sequences from extracellular matrix (ECM) and non-ECM proteins have also been identified for the first time in ancient tissue samples. These data provide a framework for analyzing ancient protein signatures in wellpreserved fossil specimens, while also contributing novel insights into the molecular basis of organic matter preservation. As such, this analysis has unearthed common posttranslational modifications of collagen that may assist in its preservation over time. During the last decade, paleontology and taphonomy (the study of decaying organisms over time and the fossilization processes) have begun to overlap with the field of proteomics to shed new light on preserved organic matter in fossilized bones (1-4). These bones represent a time capsule of ancient biomolecules, owing to their natural resistance to post mortem decay arising from a unique combination of mechanical, structural, and chemical properties (4 -7).Although bones can be cursorily described as a composite of collagen (protein) and hydroxyapatite (mineral), fossilized bones undergo three distinct diagenesis pathways: (i) chemical deterioration of the organic phase; (ii) chemical deterioration of the mineral phase; and (iii) (micro)biological attack of the composite (6). In addition, the rate of these degradation pathways are affected by temperature, as higher burial temperatures have been shown to accelerate these processes (6,8). Though relatively unusual, the first of these three pathways results in a slower deterioration process, which is more generally mitigated under (6) specific environmental constraints, such as geochemical stability (stable temperature and acidity) that promote bone mineral preservation. Importantly, slower deterioration results in more pre...

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“…One of two Roman cremations showed the presence of human albumin, as did the positive control, a sample of human serum which had been placed in a bath of boiling water for one hour; there was no cross-reactivity with cremated animal material. It is therefore thought likely that albumin, or a significant epitope, can survive at high temperatures, as has been shown already for osteocalcin (Ulrich et al, 1987). If these preliminary results are confirmed, the possibilities for future archaeological studies are clearly very exciting.…”

Section: ++mentioning

confidence: 74%

Reliable identification of human albumin in ancient bone using ELISA and monoclonal antibodies

Cattaneo

Gelsthorpe

Phillips³

et al. 1992

American J Phys Anthropol

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In order to help reconstruct ancient dietary, domestic, and ritual behaviour, a method was developed to identify the blood protein albumin in ancient skeletal material. This was an inhibition enzyme-linked immunosorbent assay (ELISA) using a monoclonal antibody of IgG class against human albumin. With fresh material, the technique gave consistent and specific results and could detect as little as 10 ng of albumin. Extracts of bone from the English Civil War (A.D. 1644), Mediaeval (A.D. 1100-1400), Early Saxon (A.D. 450-600), Roman (A.D. 100-200), Iron Age (ca 400 B.C.) and Bronze Age (2200-1700 B.C. cal.) periods were then tested, samples of fresh human and animal bone being included as positive and negative controls, respectively. Albumin was demonstrated in human bone from all periods; there was no evidence of cross-reactivity with animal material. Detection seemed to depend largely on amount of sample and chronological age; other factors, such as physical integrity of the specimen and soil characteristics, appeared to be less important. Preliminary studies of other ancient skeletal remains showed that animal species could be readily identified and that albumin was probably still detectable in cremated material. It is concluded that our method provides a tool specific and sensitive enough for the reliable identification of the species-origin of small fragments of bone (and possibly of blood stains) and will thus allow insight into past behaviour patterns. ELISA may also be suitable for identifying other molecules (such as HLA and ABO) which would help determine racial affiliation and disease predisposition among ancient populations.

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Extraction of osteocalcin from fossil bones and teeth

Cited by 52 publications

References 11 publications

Preliminary Results for the Analysis of Lipids in Ancient Bone

Preliminary Results for the Analysis of Lipids in Ancient Bone

Preserved Proteins from Extinct Bison latifrons Identified by Tandem Mass Spectrometry; Hydroxylysine Glycosides are a Common Feature of Ancient Collagen

Reliable identification of human albumin in ancient bone using ELISA and monoclonal antibodies

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