Hearing the grass grow. Emotional and epistemological challenges of practice-near research

This paper discusses the concept of practice-near research in terms of the emotional and epistemological challenges that arise from the researcher coming 'near' enough to other people for psychological processes to ensue. These may give rise in the researcher to confusion, anxiety and doubt about who is who and what is what; but also to the possibility of real emotional and relational depth in the research process. Using illustrations from three social work doctoral research projects undertaken by students at the Tavistock Clinic and the University of East London the paper examines four themes that seem to the author to be central to meaningful practice-near research undertaken in a spirit of true emotional and epistemological open-mindedness: the smell of the real; losing our minds; the inevitability of personal change; and the discovery of complex particulars

The phytochemical diversity and product quality of shea butter present confounding factors to product standardization in research

Muoghalu et al, describe the anti-inflammatory activity of whole unrefined shea butter in an animal model. This study is important because shea butter extracts have promising characteristics for treating inflammatory disorders. However, the authors did not appropriately characterise the concentration of the specific bioactive compounds identified from their literature review prior to their in vivo studies. This lack of characterisation limits ability to extrapolate the important anti-inflammatory findings more broadly

Doctrinal Evolution and the Right Against Self-Incrimination

The Fifth Amendment’s right against self-incrimination is one of the most well-known constitutional protections as it is often referenced in movies, television shows, and in the news. Despite this wide-spread awareness of the right against self-incrimination, the Federal Circuit Courts remain split over whether the right attaches before or during trial. The specific point of contention is when a “criminal case” commences. This article examines the history of the right against self-incrimination beginning with its common-law origins in Great Britain. The evolution of the right against self-incrimination is explored up to the present-day circuit split, and the cases involved in the split are discussed in detail. Finally, this article argues for a broad application of the right against self-incrimination

The Cocktail Party (January 6-7, 1961)

Program for The Cocktail Party (January 6-7, 1961)

Bioengineering the Expression of Active Recombinant Human Cathepsin G, Enteropeptidase, Neutrophil Elastase, and C-Reactive Protein in Yeast

The yeasts Pichia pastoris and Kluyveromyces lactis were used to express several recombinant human proteins for further biochemical characterization. Two substitution variants of recombinant human enteropeptidase light chain (rhEPL) were engineered to modify the extended substrate specificity of this serine protease. Both were secreted as active enzymes in excess of 1.7 mg/L in P. pastoris fermentation broth. The substitution variant rhEPL R96Q showed significantly reduced specificities for the preferred substrate sequences DDDDK and DDDDR; however, the rhEPL Y174R variant displayed improved specificities for these substrate sequences relative to all other reported variants of this enzyme. The neutrophil serine proteases human cathepsin G (hCatG) and human neutrophil elastase (HNE) were expressed in P. pastoris and HNE was also expressed in K. lactis. The recombinant variants rhCatG and rHNE, with intact C-terminal extensions, were expressed as fusion proteins with the soluble heme-binding domain of cytochrome B5 (CytB5) and an N-terminal hexahistidine (6xHis) tag for purification. The CytB5 domain was linked to the native N-termini of active rhCatG and rHNE by the EPLcleavable substrate sequence DDDDK~I, where ~ is the sessile bond. These fusion proteins were directed for secretion. The yeast P. pastoris expressed up to 3.5 mg/L of EPL-activable rHNE in fermentation broth; however, only 200 μg/L of rhCatG could be produced by this method. Recombinant expression in K. lactis never surpassed 100 μg/L of activable rHNE. The CytB5 fusion domain was present in the heme-bound form, conferring a red color and 410 nm absorbance peak to solutions containing the fusion proteins. This absorbance pattern was most readily visible during the purification of CytB5-rHNE from P. pastoris. Human C-reactive protein (hCRP) and the substitution variant CRP E42Q were expressed in recombinant form and secreted by P. pastoris. Both products were found to bind phosphocholine (PCh) in the same manner as native hCRP. Difficulties encountered during purification revealed that wild type recombinant CRP (rCRP) was produced at 2 different molecular masses. The P. pastoris recombinant expression system yielded better results than K. lactis. Bioreactor-scale fermentation in a 5 L vessel facilitated expression and characterization of these recombinant proteins