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“Protein refolding is a bottleneck in the production of therapeutic proteins from inclusion bodies In recent years several studies have described on-column refolding of recombinant proteins DT389-hIL13 is a recombinant protein that targets the glioma In our study the recombinant protein DT389-hIL13 was expressed in Escherichia coli (E colt) The Isolated inclusion bodies were refolded using size exclusion chromatography (SEC) and further purified using anion exchange chromatography Three different methods of SEC on-column refolding were studied In vitro tests on U251 cells showed that the recombinant protein could effectively inhibit the proliferation of 13251 cells especially the protein refolded by urea and pH gradient method The half-maximal IPI145 datasheet inhibitory concentration (IC50) of 0 887 nM was achieved with this new method unlike an IC50 of 11 4 nM achieved in the non-gradient method (C) 2010 Elsevier Inc All rights Ispinesib nmr reserved”
“The coxsackievirus-adenovirus receptor (CAR) and decay-accelerating factor (DAF) have been identified as cellular
receptors for coxsackievirus B3 (CVB3). The first described DAF-binding isolate was obtained during passage of the prototype strain, Nancy, on rhabdomyosarcoma (RD) cells, which express DAF but very little CAR. Here, the structure of the resulting variant, CVB3-RD, has been solved by X-ray crystallography to 2.74 angstrom, and a cryo-electron microscopy reconstruction of CVB3-RD complexed with DAF has been refined to 9.0 angstrom. This new high-resolution structure permits us to correct an error in
our previous view of DAF-virus interactions, providing a new footprint of DAF that bridges two adjacent protomers. The contact sites between the virus and very DAF clearly encompass CVB3-RD residues recently shown to be required for binding to DAF; these residues interact with DAF short consensus repeat 2 (SCR2), which is known to be essential for virus binding. Based on the new structure, the mode of the DAF interaction with CVB3 differs significantly from the mode reported previously for DAF binding to echoviruses.”
“The opioid peptides, dynorphin (DYN) and enkephalin (L-ENK) are contained in the hippocampal mossy fiber pathway where they modulate synaptic plasticity. In rats, the levels of DYN and L-ENK immunoreactivity (-ir) are increased when estrogen levels are elevated (Torres-Reveron et al., 2008, 2009). Here, we used quantitative immunocytochemistry to examine whether opioid levels are similarly regulated in wildtype (WT) mice over the estrous cycle, and how these compared to males. Moreover, using estrogen receptor (ER) alpha and beta knock-out mice (AERKO and BERKO, respectively), the present study examined the role of ERs in rapid, membrane-initiated (6 h), or slower, nucleus-initiated (48 h) estradiol effects on mossy fiber opioid levels.