Purification of highly bindable rat brain hexokinase by high performance liquid chromatography (HPLC).
Purification of highly bindable rat brain hexokinase by high performance liquid chromatography (HPLC).
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通过高效液相色谱 (HPLC) 纯化高度可结合的大鼠脑己糖激酶。
DOI：
10.1016/0006-291x(82)90613-1
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发表时间：
1982
影响因子：
3.1
通讯作者：
Wilson,JE
中科院分区：
文献类型：
--
作者：
Polakis,PG;Wilson,JE
用改进的阴离子交换柱高效液相色谱法（HPLC）代替DEAE-纤维素柱色谱法纯化了大鼠脑己糖激酶。所得酶以良好的产率获得，并且基于SDS-凝胶电泳几乎是均质的;比活性（约60单位/mg蛋白质）与DEAE纯化的酶相当。然而，与后一种酶相反，HPLC纯化的酶保留了其与线粒体结合的能力。高效液相色谱法对大鼠脑己糖激酶的结合型和非结合型具有良好的分离度。
Rat brain hexokinase has been purified by a modification of a previously described procedure in which High Performance Liquid Chromatography (HPLC) on an anion exchange column is substituted for DEAE-cellulose column chromatography. The resulting enzyme is obtained in good yield and is nearly homogeneous based on SDS-gel electrophoresis; the specific activity (about 60 units/mg protein) is comparable to the DEAE-purified enzyme. In contrast to the latter enzyme, however, the HPLC-purified enzyme retains its ability to bind to mitochondria. Excellent resolution of bindable and nonbindable forms of rat brain hexokinase is achieved with HPLC.