GPI锚定丝氨酸蛋白酶testisin的活化机制研究
Mechanistic studies on regulation of the activity of GPI-anchored serine protease testisin
Note：A. SDS-PAGE of the preliminary activation tests of mTN under reducing conditions. B. SDS-PAGE of mTN obtained by Q anion exchange chromatography under reducing conditions. C.Schematic diagram of the molecular structure of mTN with two mutation sites prominently identified. D. Activation status of mTN and the two variants was detected every 24 h. The relative activity of mTN was derived from slope of the linear plot of absorbance at 405 nm vers incubation time during activity assay. Western blotting analysis revealed that a band of approximately 5 000 corresponded to the zymogen, while a band of approximately 1 500 corresponded to the degraded C-terminal fragment.
