Abstract
<p class="IsiAbstrakIndo"><span lang="EN-GB">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. </span></p>
Highlights
Tuberculosis still poses a significant threat to global health
The present study focuses on the Tyrosine phosphatase B (PtpB)
Materials Escherichia coli strain XL1-Blue was used for cloning and strain BL21(DE3) was used for expression
Summary
Tuberculosis still poses a significant threat to global health. In contrast to the significant reduction of global TB cases over past two decades (Chapman & Lauzardo, 2014), the figure in some regions is still beyond expectation. In Indonesia, for example, TB case is still high. A recent report suggested that over a million cases are found in the archipelagic country with mortality may as high as 45% and economic loss of about USD 6.9 billion (Collins et al, 2017). Vaccination against TB has long been implemented, its efficacy is a controversial matter. An array of new vaccines is currently on the horizon, but they will not be available in short time (Parida & Kaufmann, 2010)
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