人肝线粒体天冬氨酸氨基转移酶提纯及比活性研究  

PURIFICATION AND SPECIFIC ACTIVITY OF MITOCHONDRIAL ASPARTATEAMINO TRANSFERASE FROM HUMAN LIVER

在线阅读下载全文

作  者:李绍冰[1] 魏素珍[2] 方丁 

机构地区:[1]河北省人民医院老年病科 [2]河北医科大学基础所

出  处:《河北医科大学学报》1998年第3期149-152,共4页Journal of Hebei Medical University

摘  要:目的:建立人肝线粒体型天冬氨酸氨基转移酶(mAST)提纯方法,制备兔抗人mAST抗血清,为免疫法测定人血清mAST作准备。方法:采用DEAE纤维素柱层析及亲和层析从人肝中提纯mAST。应用淋巴结注射法制备兔抗人mAST抗血清。结果:mAST比活为300000U/mg蛋白,达到电泳纯和免疫纯,抗血清效价为1∶16。结论:DEAE纤维素柱层析及亲和层析能够制备高纯度人mAST,制备的兔抗人mAST抗血清效价较高,为建立免疫方法测定mAST创造了条件。Objective:To establish the methods for the purification of mAST and prepare rabbit antiserum against human mAST so as to set the basis for the measurement of human serum mAST with immunomethod.Methods:The mAST was purified by DEAEcellulose column chromatography and affinity chromatography from human liver.Results:The specific activity of purified mAST is 300 000U/mg protein.The preparation of mAST was identified to be homogeneous by SDSPAGE,PAGE and immunomethod.The titer of the rabbit antihuman mAST serum was 1∶16.Conclusion:Human liver mAST can be highly purified by DEAEcellulose column chromatography and affinity chromatography.The purified mAST and antiserum are of great value in the measurement of human serum mAST by immunomethod.

关 键 词:肝线粒体 天冬氨酸 氨基转移酶 提纯m-AST 

分 类 号:Q555.03[生物学—生物化学]

 

参考文献:

正在载入数据...

 

二级参考文献:

正在载入数据...

 

耦合文献:

正在载入数据...

 

引证文献:

正在载入数据...

 

二级引证文献:

正在载入数据...

 

同被引文献:

正在载入数据...

 

相关期刊文献:

正在载入数据...

相关的主题
相关的作者对象
相关的机构对象