U. Weser et Y. Kaup, INTACT MUMMIFIED BONE ALKALINE-PHOSPHATASE, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1208(1), 1994, pp. 186-188
Our knowledge to the mode of conservation of mummified structurally an
d functionally intact biopolymers is limited. Rib samples of a well-pr
eserved 2300-year old ptolemeic mummy were examined whether or not fun
ctionally active Zn2Mg alkaline phosphatase could be detected. A prote
in of M(r) 170 +/- 20 kDa being close to 200 kDa of the enzyme of fles
h bones was successfully isolated. Both a 200 kDa protein and a distin
ct subunit of 60 kDa were seen in SDS-PAGE electrophoresis which was i
dentical to those of fresh bone alkaline phosphatase. There was a sign
ificant enzymic activity of 17 mU/mg protein which could be inhibited
in the presence of L-homoarginine and 1,10-phenanthroline.