BIOCHEMICALLY AND IMMUNOLOGICALLY ACTIVE ALKALINE-PHOSPHATASE IN ARCHAEOLOGICALLY IMPORTANT BONE SAMPLES

Bone samples of different archaeological sites and age have been emplo yed to examine both the possible catalytic and immunological activity of Zn(M)g alkaline phosphatase. In six samples a protein of Mr 180 +/- 20 kD being close to 200 kD of the contemporary enzyme was successful ly isolated. The specific enzymic activity ranged from 5 to 100 mU/mg protein. In the presence of the inhibitors 1,10-phenanthroline and L-h omoarginine the enzymic activity was diminished. Likewise heating to 1 00 degrees C and replacement of Zn(II) by Cd(II) resulted in a dramati c loss of activity. Distinct immunological activity against the human enzyme was demonstrated in the Superdex 200 gel filtrate of one Anglo- Saxon femur bone (Bidwell, UK, AD 429-664) extract.