title: Characterization and purification of acid phosphatase from ancient human bone.
abstract: In this research, acid phosphatase was purified and characterized from approximately 3000-year-old human bones from archeological excavations. Using anion exchange chromatography, two isoenzymes, TrACP and TsACP, were isolated from the bone. TrACP and TsACP were eluted separately, with a concentration gradient, from a CM-sepharose column. The resulting TrACP was further purified on a cellulose phosphate column. The activity was determined by using pNPP as substrate. Additionally, protein was determined by the Bradford and Coomassie Brilliant Blue method. The optimum pHs of TsACP and TrACP were 6 and 5, respectively. The optimum temperatures were 0 and 10 degrees C, respectively. Molecular weights were measured by gel filtration chromatography. The isoenzyme purity was checked with SDS-PAGE. Finally, the effects of sodium molybdate and tartrate on isoenzyme activity were determined.
authors: Department of Chemistry, Atatürk University, Erzurum, Turkey.
authors: Yaşar
authors: Y
authors: Demir
authors: Safinur
authors: S
authors: Yildirim
authors: Azize
authors: A
authors: Alayli
authors: Nazan
authors: N
authors: Demir
mesh_terms: D000135:Acid Phosphatase / Q000737:chemistry / Q000266:history / Q000302:isolation & purification*; D001842:Bone and Bones / Q000201:enzymology*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D049690:History, Ancient; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification; D008970:Molecular Weight; D000071681:Tartrate-Resistant Acid Phosphatase; D013696:Temperature
chemical_list: D007527:Isoenzymes; D000135:Acid Phosphatase; D000071681:Tartrate-Resistant Acid Phosphatase