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Intact mummified bone alkaline phosphatase

U Weser¹, Y Kaup

¹Department of Inorganic Biochemistry, University of Tübingen, Germany.

Biochimica Et Biophysica Acta

|September 21, 1994

Summary

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Researchers detected active alkaline phosphatase, an enzyme crucial for bone health, in a 2300-year-old mummy. This finding offers new insights into the preservation of biopolymers in ancient remains.

Area of Science:

Biochemistry
Paleopathology
Biopolymer preservation

Background:

Understanding the long-term preservation of functional biopolymers in mummified remains is limited.
Ancient Egyptian mummification techniques offer a unique window into post-mortem biomolecular stability.

Purpose of the Study:

To investigate the presence and activity of alkaline phosphatase (ALP) in a 2300-year-old Ptolemaic mummy.
To determine if functionally intact biopolymers can be conserved over millennia.

Main Methods:

Analysis of rib bone samples from a well-preserved Ptolemaic mummy.
Isolation and characterization of proteins using SDS-PAGE electrophoresis.
Enzymatic activity assays and inhibition studies.

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Main Results:

A protein of approximately 170 kDa, close to the molecular weight of fresh bone ALP (200 kDa), was isolated.
SDS-PAGE revealed a 200 kDa protein and a 60 kDa subunit identical to fresh bone ALP.
Significant enzymatic activity (17 mU/mg protein) was detected, inhibitable by L-homoarginine and 1,10-phenanthroline.

Conclusions:

Functionally active alkaline phosphatase can be preserved in mummified human bone for over 2300 years.
This study demonstrates the remarkable stability of certain biopolymers under mummification conditions.
The findings contribute to our understanding of biomolecular degradation and preservation in ancient tissues.