Ito K, Yamamoto H, Mizugaki M
Department of Pharmaceutical Sciences, Tohoku University Hospital, Miyagi.
J Biochem. 1988 Feb;103(2):259-62. doi: 10.1093/oxfordjournals.jbchem.a122257.
AMP deaminase from sheep brain was purified to homogeneity on SDS-PAGE and its general properties were investigated. The native enzyme has a molecular weight of approximately 350,000 as estimated by gel filtration and it is composed of four identical subunits with a molecular weight of 85,000 each. The purified enzyme had a specific activity of 500 units/mg protein and shows a sigmoid-shaped AMP saturation curve in the presence of 100 mM KCl. This deaminase is strongly activated by ATP and inhibited by GTP. It slightly catalyzes the hydrolysis of adenosine monosulfate (AMS), dAMP, and adenosine phosphoramidate (APA). These catalytic properties resemble those of AMP deaminase from human liver.
从羊脑中纯化出的AMP脱氨酶在SDS-PAGE上达到了均一性，并对其一般性质进行了研究。通过凝胶过滤估计，天然酶的分子量约为350,000，它由四个相同的亚基组成，每个亚基的分子量为85,000。纯化后的酶比活性为500单位/毫克蛋白质，在100 mM KCl存在下呈现S形的AMP饱和曲线。这种脱氨酶受到ATP的强烈激活，被GTP抑制。它能轻微催化单磷酸腺苷（AMS）、dAMP和腺苷磷酰胺（APA）的水解。这些催化特性与人肝中的AMP脱氨酶相似。
