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本文将共价偶联于CNBr活化的Sepharose 4B上的烟草核酮糖-1,5-二磷酸羧化酶/加氧酶用不同浓度尿素处理后,发现2—2.5mol/L尿素可将小亚单位解离下来而大亚单位仍偶联在载体上。3mol/L以上尿素可将大亚单位8聚体,L_8进一步解离为单体。因此,酶是通过大亚单位上的ε-氨基与载体相偶联的。小亚单位的解离量与酶活性的下降呈线性相关。将解离酶的尿素浓度稀释至0.5mol/L,解离的小亚单位几乎全部结合到残缺小亚单位的固相酶上,酶的活性也接近全部恢复。重组小亚单位量与酶活性增加亦呈线性相关。结果表明:除大亚单位外,小亚单位对维持酶的活性也有重要的作用。
This paper covalently coupled to CNBr-activated Sepharose 4B ribulose-1,5-bisphosphate carboxylase / oxygenase with different concentrations of urea treatment and found that 2-2.5mol / L urea can be small Subunits dissociate and large subunits are still coupled to the carrier. 3mol / L of urea can be a large subunit 8-mer, L_8 further dissociation into monomers. Therefore, the enzyme is coupled to the carrier through the epsilon-amino group on the large subunit. The amount of dissociation of small subunits was linearly correlated with the decrease of enzyme activity. The dissociation enzyme concentration of urea diluted to 0.5mol / L, the dissociation of small subunits almost completely bonded to the defective small subunit of the solid phase enzyme, the enzyme activity is also close to fully recovered. The amount of recombinant small subunit was also linearly correlated with the increase of enzyme activity. The results showed that besides the large subunit, small subunits also play an important role in maintaining enzyme activity.