Abstract：
:Frontal affinity chromatography (FAC) combined with enzyme has been widely used for drug screening. In this paper, the effect of target enzyme activity on screening of bioactive compounds was studied through applying FAC. Trypsin with different degree of inactivation were prepared as target enzyme by thermal denaturation. Their primary structure was identified by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and use Fourier transform infrared (FTIR) and ultraviolet-visible (UV-vis) spectroscopy to detect group structure. Ultimately, it was found that the main structure of enzyme with decreased activity remained unchanged. The oxymatrine and matrine which can interact with trypsin were selected to study their binding to trypsin with different activities in FAC. The results showed that oxymatrine and matrine had a significant difference in the breakthrough volume among seven kinds of columns prepared by trypsins with different activities, at the different concentration. It indicated that trypsins with different activities in FAC could combine with oxymatrine and matrine. The binding constant (Kd) variation between oxymatrine, matrine and trypsin with different activities are 5.520 ± 0.038 and 3.577 ± 0.071, within error range, which indicated that the activity of target enzyme with primary unchanged structure has no effect on screening of bioactive components by FAC.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Qian J,Zhao C,Tong J,Jiang S,Zhang Z,Lu S,Guo Hdoi
10.1016/j.ijbiomac.2019.07.218subject
Has Abstractpub_date
2019-10-15 00:00:00pages
740-751eissn
0141-8130issn
1879-0003pii
S0141-8130(19)34777-4journal_volume
139pub_type
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