Author:
Kaup Yoka,Baumer Ursula,Koller Johann,Hedges Robert E. M.,Werner Herbert,Hartmann Hans-Jürgen,Etspüler Hedwig,Weser Ulrich
Abstract
Bone samples of a ptolemeic mummy have been employed to study the mode of conservation on the intactness of Zn2Mg alkaline phosphatase in both structure and catalytic activity. A protein of Mr = 190 ± 10 kDa being identical to the 200 kDa enzyme of fresh human bones was successfully isolated. Regardless of age 200 kDa protein bands and a distinct sub unit at 60 kDa were seen in SDS-PAGE electrophoresis. The 200 kDa band was also monitored by activity staining. The specific activity was 120 mU/mg and 65% of the respective activity obtained in the identical preparation using fresh human tibia or rib. The enzymic activity was inhibited in the presence of 1,10-phenanthroline and ʟ-homoarginine. Radiocarbon dating supported the assignment of the mummy to the early ptolemeic period. Among the many bactericidal and fungicidal components employed for mummification were aromatic alcohols, mono-and sesquiterpenes. Pistachio resin was the major balm resin used. The microbiological sterility of the bone surface was ascertained by independent bacterial and fungal examinations
Subject
General Biochemistry, Genetics and Molecular Biology
Cited by
15 articles.
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