Intact mummified bone alkaline phosphatase.
Our knowledge to the mode of conservation of mummified structurally and functionally intact biopolymers is limited. Rib samples of a well-preserved 2300-year old ptolemeic mummy were examined whether or not functionally active Zn2Mg alkaline phosphatase could be detected. A protein of M(r) 170 +/- 20 kDa being close to 200 kDa of the enzyme of fresh bones was successfully isolated. Both a 200 kDa protein and a distinct subunit of 60 kDa were seen in SDS-PAGE electrophoresis which was identical to those of fresh bone alkaline phosphatase. There was a significant enzymic activity of 17 mU/mg protein which could be inhibited in the presence of L-homoarginine and 1,10-phenanthroline.
Weser
U
U
Department of Inorganic Biochemistry, University of Tübingen, Germany.
Kaup
Y
Y
D000469:Alkaline Phosphatase / Q000032:analysis* / Q000037:antagonists & inhibitors; D001842:Bone and Bones / Q000201:enzymology*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D008274:Magnesium; D008970:Molecular Weight; D009106:Mummies; D015032:Zinc
D000469:Alkaline Phosphatase; D008274:Magnesium; D015032:Zinc