Monoclonal antibodies recognize 2300 years aged alkaline phosphatase.
It was attempted to monitor the immunological response of monoclonal antibodies directed to human alkaline phosphatase in ancient Egyptian bones from the ptolemeic period. The intactness of the respective epitopes of the bone enzyme was successfully demonstrated in an ELISA. Fortunately, the mummified bone was not contaminated by fungi and bacteria due to the fungicidal and bactericidal reactivity of the ancient pretreatment employing resins of pistachio for mummification. The enzyme was enriched using gel chromatography, anion exchange and affinity chromatography to yield 310 +/- 7 mU/mg. The enzymically active fractions of the wheat-germ lectin affinity chromatography were subjected to ELISA. The best binding affinity was detected using the monoclonal antibody BAP A while the reactions of all the other four antibodies BAP B, BAP G, BAP 4A5 and BAP 5D4 were substantially diminished.
Etspüler
H
H
Anorganische Biochemie, Physiologisch Chemisches Institut, Universität Tübingen, Germany.
Kaup
Y
Y
Bailyes
E M
EM
Luzio
J P
JP
Weser
U
U
D000469:Alkaline Phosphatase / Q000737:chemistry / Q000276:immunology* / Q000302:isolation & purification; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D005260:Female; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D009106:Mummies / Q000473:pathology*
D000911:Antibodies, Monoclonal; D000469:Alkaline Phosphatase