大鼠前脑神经末梢胞质溶胶中的胆碱激酶和乙醇胺激酶活性。
Choline kinase and ethanolamine kinase activity in the cytosol of nerve endings from rat forebrain.
作者信息
Spanner S, Ansell G B
出版信息
Biochem J. 1979 Mar 15;178(3):753-60. doi: 10.1042/bj1780753.
Abstract
Both choline kinase and ethanolamine kinase are present in the cytosol of nerve endings prepared from rat brain are the products of their action, phosphocholine (84 nmol/g fresh wt. of brain) and phosphoethanolamine (190 nmol/g fresh wt. of brain). In contrast with the enzymes from the cytosol of whole brain, both are as equally active at pH 7.5 as 9.0. Determination of kinase activity in membrane-containing tissue samples at pH9 gives low values because of the activity of alkaline phosphatase. Choline kinase, but not ethanolamine kinase, requires Mg2+ in excess of that required for the formation of the MgATP complex and is inhibited by an excess of free ATP. The Km for choline is 2.6mM and for ethanolamine is 2.2mM. The differing requirements for ATP and Mg2+ and the inhibition of choline kinase, but not ethanolamine kinase, by hemicholinium-3 suggest either the presence of two separate enzymes or two different active sites on the same enzyme.
摘要
胆碱激酶和乙醇胺激酶都存在于从大鼠脑中制备的神经末梢的胞质溶胶中，它们作用的产物分别是磷酸胆碱（84纳摩尔/克脑鲜重）和磷酸乙醇胺（190纳摩尔/克脑鲜重）。与全脑胞质溶胶中的酶不同，这两种酶在pH 7.5和pH 9.0时的活性相同。由于碱性磷酸酶的活性，在pH 9下测定含膜组织样品中的激酶活性会得到较低的值。胆碱激酶，但不是乙醇胺激酶，需要的镁离子超过形成MgATP复合物所需的量，并且会被过量的游离ATP抑制。胆碱的Km为2.6毫摩尔，乙醇胺的Km为2.2毫摩尔。对ATP和镁离子的不同需求以及半胱氨酸-3对胆碱激酶而非乙醇胺激酶的抑制表明，要么存在两种不同的酶，要么在同一种酶上存在两个不同的活性位点。
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