发育中的玉米种子中ADP-葡萄糖焦磷酸化酶A的纯化与特性分析
The purification and characterization of ADP-glucose pyrophosphorylase A from developing maize seeds.
作者信息
Fuchs R L, Smith J D
出版信息
Biochim Biophys Acta. 1979 Jan 12;566(1):40-8. doi: 10.1016/0005-2744(79)90246-8.
ADPglucose pyrophosphorylase A (ATP:alpha-D-glucose-1-phosphate adenylyltransferase, EC 2.7.7.27) from developing maize (Zea mays) endosperm was purified 129 fold to apparent homogeneity. The molecular weight estimated by gel filtration and by polyacrylamide gel electrophoresis was 375 000 and 400 000, respectively. The preparation gave a single protein band after SDS-polyacrylamide gel electrophoresis suggesting a monomer mol. wt. of 96 000. It was concluded that ADPglucose pyrophosphorylase A in maize endosperm is a tetramer of four similar molecular weight subunits. Values for the Km for glucose 1-phosphate and ATP were 3.8 . 10(-5) and 1.8 . 10(-4) M, respectively (using the homogeneous preparation).
从发育中的玉米（Zea mays）胚乳中纯化出的ADP葡萄糖焦磷酸化酶A（ATP：α-D-葡萄糖-1-磷酸腺苷酰转移酶，EC 2.7.7.27），纯化倍数达129倍，达到表观均一。通过凝胶过滤和聚丙烯酰胺凝胶电泳估计的分子量分别为375000和400000。该制剂在SDS-聚丙烯酰胺凝胶电泳后呈现单一蛋白条带，表明单体分子量为96000。得出的结论是，玉米胚乳中的ADP葡萄糖焦磷酸化酶A是由四个分子量相似的亚基组成的四聚体。1-磷酸葡萄糖和ATP的Km值分别为3.8×10⁻⁵和1.8×10⁻⁴M（使用均一制剂）。
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