The Purification and characterization of alkalene phosphatase enzyme in ancient human and Northern Anatolia steppe elephant (elephas trogontherii-mammoth) bones

II SUMMARY Human bone alkaline phosphatase was isolated and its characteristic features were determined. In according to bonding forms, AP enzymes were separately purified and characterized at four steps from steps elephant (Elephas Trogontherii) as outer peripheral, inner peripheral, integral and cytosolic. Using gel filtration and anion exchange chromatography purified human bone alkaline phosphatase enzyme that aged 3000 years. 0,3-0,8 million years aged elephant bone alkaline phosphatase isoenzymes was purified by using anion exchange chromatography. The activity measurement of these izoenzymes was used by using p- nitrophenylphosphate as substrate. The optimum pH and the optimum temperatures of AP izoenzymes were determined. The behaviors of AP against Ca+2 and tonocalsin has been investigated. The molecular weight of all enzymes was determinated by using gel filtration. Also Vmax and Km values of purified isoenzymes from human and elephant bone were found by using Lineweaver-Burk method. Human bone AP and elephant bone AP izoenzymes were characterized based on the obtained results.