Crystallization of human liver alcohol dehydrogenase.
Crystallization of human liver alcohol dehydrogenase.
复制标题
人肝乙醇脱氢酶的结晶。
DOI：
10.1016/0003-9861(67)90097-5
复制
发表时间：
1967
影响因子：
3.9
通讯作者：
C. Woronick
中科院分区：
文献类型：
--
作者：
N. Mourad;C. Woronick
乙醇脱氢酶是从人的肝脏中结晶出来的。纯化过程包括：硫酸铵分级，乙醇-氯仿处理，Car☐甲基纤维素层析和二乙氨基乙基纤维素层析，乙醇结晶。经超速离心法和圆盘电泳法鉴定，结晶蛋白均一。这种酶是一种碱性蛋白质。氨基酸分析表明，碱性氨基酸多于酸性氨基酸。在本实验条件下，人肝乙醇脱氢酶的活性约为马肝乙醇脱氢酶的71%。
Alcohol dehydrogenase has been crystallized from human liver. The purification procedure consisted of fractionation with ammonium sulfate, treatment with ethanol-chloroform, chromatography on car☐ymethylcellulose and on diethylaminoethyl-cellulose, and crystallization from aqueous ethanol. The crystalline protein was found to be homogeneous by ultracentrifugation and by disc electrophoresis. The enzyme is a basic protein. Amino acid analysis showed that there is an excess of basic amino acids over acidic amino acids. Under the conditions of the assay, human liver alcohol dehydrogenase is about 71% as active as horse liver alcohol dehydrogenase.