玉米叶片中磷酸葡萄糖变位酶和磷酸甘露糖变位酶的纯化、分离及特性分析
Purification, separation and characterization of phosphoglucomutase and phosphomannomutase from maize leaves.
作者信息
Popova T N, Matasova L V, Lapot'ko A A
机构信息
Department of Plant Physiology and Biochemistry, Voronezh State University, Russia.
出版信息
Biochem Mol Biol Int. 1998 Oct;46(3):461-70. doi: 10.1080/15216549800203982.
Different phosphomutases-phosphoglucomutase (EC 2.7.5.1; PGM) and phosphomannomutase (EC 2.7.5.7; PMM) from maize (Zea mays L.) leaves have been purified. PGM and PMM were completely separated from each other. The purified PGM was shown to be electrophoretically homogeneous. The PGM from maize leaves was found to be a homodimer with an apparent molecular mass of 132 kDa, the size of the subunits was 66 kDa. The PGM is a bifunctional enzyme, which can use both glucose-1-phosphate and mannose-1-phosphate as substrates. In contrast, the PMM appears to be monospecific for mannose-1-phosphate. Evidence is presented that PMM differs from PGM. Some properties of the maize leaves PGM and PMM differ in many respects (K(m) for substrates, pH optimum). However, some properties of PGM and PMM were similar (influence of Mg2+ and Mn2+ ions).
已从玉米（Zea mays L.）叶片中纯化出不同的磷酸变位酶——磷酸葡萄糖变位酶（EC 2.7.5.1；PGM）和磷酸甘露糖变位酶（EC 2.7.5.7；PMM）。PGM和PMM已完全彼此分离。纯化后的PGM经电泳显示为均一的。发现玉米叶片中的PGM是一种同型二聚体，表观分子量为132 kDa，亚基大小为66 kDa。PGM是一种双功能酶，它既能利用葡萄糖-1-磷酸又能利用甘露糖-1-磷酸作为底物。相比之下，PMM似乎对甘露糖-1-磷酸具有专一性。有证据表明PMM与PGM不同。玉米叶片PGM和PMM的一些特性在许多方面存在差异（底物的K(m)、最适pH）。然而，PGM和PMM的一些特性是相似的（Mg2+和Mn2+离子的影响）。
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