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首页> 外文期刊>Preparative biochemistry & biotechnology: An international journal for rapid communication >Characterization and Purification of Acid Phosphatase from Ancient Human Bone
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Characterization and Purification of Acid Phosphatase from Ancient Human Bone

机译：古代人骨中酸性磷酸酶的表征和纯化

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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 fro mthe 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.Additioanlly,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 deg 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.
机译：在这项研究中，从考古发掘的大约3000年历史的人类骨骼中纯化并鉴定了酸性磷酸酶。使用阴离子交换色谱法从骨骼中分离出两种同功酶TrACP和TsACP，分别将TrACP和TsACP洗脱从CM-琼脂糖凝胶柱上分离浓度梯度，将所得的TrACP在纤维素磷酸酯柱上进一步纯化。以pNPP为底物测定活性。另外，用Bradford和Coomassie亮蓝法测定蛋白质。 TsACP和TrACP分别为6和5，最适温度分别为0和10摄氏度。通过凝胶过滤色谱法测量分子量。通过SDS-PAGE检查同工酶纯度。最后，钼酸钠和酒石酸盐的作用测定同工酶活性。

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