Institut für Pflanzenphysiologie, Zellbiologie und Mikrobiologie, Freie Universität Berlin, Königin-Luise-Str. 12-16a, D-1000 Berlin 33 (West).
Plant Physiol. 1988 May;87(1):78-82. doi: 10.1104/pp.87.1.78.
Aldolase activity of Chara foetida (Braun) could be separated into a minor (peak I) and a major peak (peak II) by ion-exchange chromatography on DEAE-cellulose. Affinity chromatography on P-cellulose resulted in highly purified aldolase preparations with specific activities of 3.2 and 4.8 units per milligram protein and molecular subunit masses of 37 and 35 kilodalton, as shown by SDS-PAGE, for the aldolase of peak I and peak II, respectively. Both aldolases belong to class I aldolase since the activity is not inhibited by 1 millimolar EDTA. The K(m) (fructose-1,6-bisphosphate) values were 0.64 and 13.4 micromolar, respectively. The aldolase of peak I showed a 6.7 times stronger crossreaction with a specific antiserum against the cytosol aldolase of spinach than with an antiserum against the chloroplast aldolase of spinach. On the other hand the aldolase of peak II showed a 5.1 times stronger cross-reaction with the alpha-plastidaldolase antiserum than with the alpha-cytosol-aldolase antiserum. For algae this is the first separation of two class I aldolases. They are similar to the cytosol and chloroplast aldolases in higher plants, but different from a reported class I (Me(2+) independent) and class II (Me(2+) dependent) aldolase in other algae.
淡水轮藻的醛缩酶活性可通过 DEAE-纤维素离子交换层析分离成一个次要峰（峰 I）和一个主要峰（峰 II）。P-纤维素亲和层析导致醛缩酶制剂高度纯化，其比活性分别为 3.2 和 4.8 单位/毫克蛋白，亚基分子量分别为 37 和 35 千道尔顿，如 SDS-PAGE 所示，分别为峰 I 和峰 II 的醛缩酶。这两种醛缩酶都属于 I 类醛缩酶，因为其活性不受 1 毫摩尔 EDTA 的抑制。K(m)（果糖-1,6-二磷酸）值分别为 0.64 和 13.4 微摩尔。峰 I 的醛缩酶与菠菜胞质醛缩酶的特异性抗血清的交叉反应比与菠菜叶绿体醛缩酶的抗血清强 6.7 倍。另一方面，峰 II 的醛缩酶与叶绿体α-醛缩酶抗血清的交叉反应比与胞质α-醛缩酶抗血清强 5.1 倍。对于藻类来说，这是首次分离出两种 I 类醛缩酶。它们与高等植物中的胞质和叶绿体醛缩酶相似，但与其他藻类中报道的 I 类（Me2+ 非依赖性）和 II 类（Me2+ 依赖性）醛缩酶不同。
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