Earticle

This paper explores Eugene’s Lowery’s homiletical method, focusing on the sermonic plot. Contrary to preachers who mostly follow the deductive preaching method, which mostly places its weigh on the authority of the text or of the preacher, Lowery’s homiletical method presents a room for the listeners during the preaching moment. By focusing specifically on his homiletical method, this study examines how to create a room for listeners who prefer conversational and participatory communication. It explores how sermon can be understood as a narrative art form consisting of four stages: conflict, complication, the reversal, and unfolding. This approach to the text helps the congregant interact with the text and participate in the world where the text opens. Moreover, it examines the potential of moving from a traditional, propositional way of preaching toward one that fosters audience participation and emphasizes narrative engagement. Lastly, this paper presents a practical application of preaching in which Lowry’s preaching methods can be applied to sermon preparation with detailed explanations.

The newly discovered Th2 pro-inflammatory cytokine, interleukin-17E belongs to the member of IL-17 family. In this study, bioactive recombinant mutated human IL–17E (rhIL–25) was synthesized using overlapping PCR strategy and amino acid mutations were carried out using site directed mutagenesis. Four cysteins at 78th, 83rd, 136th and 138th positions were involved in disulphide bond formation and were responsible for biological activity of mature protein. These four cysteins were replaced with serine using nucleotide substitution and the desired outcome was cloned into expression vector pRSET-A followed by expressed in a salt inducible Escherichia coli GJ1158. The transformants were selected by ampicillin resistance marker and also by DNA sequencing. SDS–PAGE analysis confirms 17.06 kDa purified protein against low molecular weight protein marker. Protein quantification was carried out using Lowry’s method. Approximately 104 mg/L of recombinant IL-17E was produced at 37 ℃. Biological activity of protein was determined by the release of IL–6 from PBMC cells using rhIL–17E. This is the first report on production of interleukin-17E structural variant with enhanced specific activity without compromising the biological activity.