Formation of complexes of Rubisco-Rubisco activase from La3+, Ce3+ treatment spinach

The complex of Rubisco and Rubisco activase from LaCl3™, CeCl3™ treated spinachin vivo is induced. SDS-PAGE result shows that the purified proteins from LaCl3™, CeCl3™ treated spinach have not only large and small subunits (55 kD, 14.4 kD) of Rubisco, but also two large subunits of 45 kD and 41 kD near the large subunits of Rubisco. Native-PAGE shows that the purified proteins from LaCl3™, CeCl3™ treated spinach have not only a band of Rubisco (560 kD), but also a band of about 1100 kD, about twice distant from Rubisco, which might be a complex of Rubisco and Rubisco activase. The purified enzyme activities from LaCl3™, CeCl3™ treated spinach are 1.8 and 2.8 times that of the control, the intensities of absorption and fluorescence are significantly higher than that of the purified Rubisco from the control, and the total sulfhydryl groups and available sulfhydryl groups are 36–39 ™SH per mol enzyme, 14–25 ™SH per mol enzyme more than those of the purified Rubisco from the control, respectively. The CD spectra show that the secondary structure of the purified enzyme from LaCl3™, CeCl3™ treated spinach is very different from the control. The enzyme activities from LaCl3™, CeCl3™ treated spinachin vivo are 1.5 and 1.9 times those of the control.