Draus E, Niefind J, Vietor K, Havsteen B
Abteilung Allgemeine Pädiatrie und Universität Kiel, F.R.G.
Biochim Biophys Acta. 1990 Aug 6;1045(3):195-204. doi: 10.1016/0005-2760(90)90120-m.
Ethanolamine kinase was purified from human liver to apparent homogeneity and its properties were studied. The minimum molecular weight of the purified enzyme was estimated by SDS-PAGE to 42,000 +/- 2000 Da. The molecular weight of the native enzyme determined by Superose 12 (FPLC) gel filtration was 87,000 +/- 4000 Da, suggesting that ethanolamine kinase in human liver consists of two chains of the same or almost the same molecular weight. The titration of the active site normality showed 1.03 +/- 0.05 active sites/chain. The Km value for ethanolamine was 0.25 +/- 0.01 mM.
从人肝脏中纯化出乙醇胺激酶至表观均一，并对其性质进行了研究。通过SDS - PAGE估计纯化酶的最小分子量为42,000±2000 Da。用Superose 12（FPLC）凝胶过滤法测定的天然酶分子量为87,000±4000 Da，这表明人肝脏中的乙醇胺激酶由两条分子量相同或几乎相同的链组成。活性位点当量滴定显示每条链有1.03±0.05个活性位点。乙醇胺的Km值为0.25±0.01 mM。
