Su H, Moniakis J, Newman E B
Biology Department, Concordia University, Montreal, Canada.
Eur J Biochem. 1993 Feb 1;211(3):521-7. doi: 10.1111/j.1432-1033.1993.tb17578.x.
The purification by affinity chromatography of beta-galactosidase from strains carrying sdaA/lacZ gene fusions results in the copurification of L-serine deaminase 1. We conclude that sdaA is the structural gene for the latter enzyme. The purified L-serine deaminase 1 obtained after collagenase treatment of an sdaA-collagen-lacZ fusion differs from the native enzyme by the addition of several amino acids at the C-terminal. Like the enzyme in crude extracts, this purified enzyme is catalytically inactive, and is activated by incubation with iron and dithiothreitol.
从携带sdaA/lacZ基因融合体的菌株中通过亲和层析法纯化β-半乳糖苷酶时，会导致L-丝氨酸脱氨酶1的共纯化。我们得出结论，sdaA是后一种酶的结构基因。用胶原酶处理sdaA-胶原-lacZ融合体后得到的纯化L-丝氨酸脱氨酶1与天然酶的不同之处在于其C末端添加了几个氨基酸。与粗提物中的酶一样，这种纯化酶没有催化活性，通过与铁和二硫苏糖醇一起温育可被激活。
