Incharoensakdi A, Takabe T, Takabe T, Akazawa T
Biochem Biophys Res Commun. 1985 Jan 31;126(2):698-704. doi: 10.1016/0006-291x(85)90241-4.
The catalytic core (A8) and small subunit (B) of ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) were isolated from two species of cyanobacteria (Aphanothece halophytica and Synechococcus ACMM 323) as well as from the photosynthetic purple sulfur bacterium, Chromatium vinosum. The subunit B is essential for the activity of all three enzymes. The heterologous hybridization of RuBisCO molecules from the three organisms was attempted and the reconstitution of the catalytically active hybrid was achieved between A8 derived from either Aphanothece or Synechococcus and subunit B from Aphanothece, Synechococcus or Chromatium. However, reconstitution of the enzymically active hybrid between A8 from Chromatium and B subunits from the cyanobacteria could not be achieved. Experiments by using high performance liquid column chromatography also showed the formation of a heterologous hybrid possessing RuBP carboxylase activity.
从两种蓝细菌（嗜盐隐杆藻和聚球藻ACMM 323）以及光合紫色硫细菌嗜硫色杆菌中分离出1,5-二磷酸核酮糖羧化酶/加氧酶（RuBisCO）的催化核心（A8）和小亚基（B）。亚基B对所有这三种酶的活性至关重要。尝试了这三种生物体的RuBisCO分子的异源杂交，并在源自嗜盐隐杆藻或聚球藻的A8与来自嗜盐隐杆藻、聚球藻或嗜硫色杆菌的亚基B之间实现了具有催化活性的杂种的重构。然而，无法实现嗜硫色杆菌的A8与蓝细菌的B亚基之间的酶活性杂种的重构。使用高效液相柱色谱法进行的实验还表明形成了具有RuBP羧化酶活性的异源杂种。
