期刊名称：Biosaintifika: Journal of Biology & Biology Education
印刷版ISSN：2085-191X
电子版ISSN：2338-7610
出版年度：2017
卷号：9
期号：3
页码：530-536
DOI：10.15294/biosaintifika.v9i3.12384
语种：English
出版社：Universitas Negeri Semarang
摘要：The present study aims at expressing and partially purifying PtpB in active form. To achieve this, Mtb PtpB gene has been cloned into pET30a vector and overexpressed in Escherichia coli BL 21(DE3) under IPTG induction in the form of an inclusion body. Following resolubilization by urea and dialysis, the resulted PtpB has been shown to be active against para-Nitrophenyl phosphate. It is concluded that the resulted PtpB has had been recovered from inclusion body to give the active form of the enzyme, and thus the success in overexpressing PtpB provides the required material to investigate the biochemical properties of the pathogen virulence factor further.
