Bedlam in mind: seeing and reading historical images of madness

In this article I explore mythical Bedlam of popular imaginings. London's Bethlem Hospital was for centuries a unique institution caring for the insane and its alter ego 'Bedlam' influenced popular stereotypes of insanity. For instance, while the type of vagrant beggar known as a 'Tom of Bedlam' was said to have disappeared from English society with the Restoration, the figure of Mad Tom retained a visual and vocal presence within popular musical culture from the seventeenth century up to the present era. Using the ballad 'Mad Tom o' Bedlam' as a case study, I illustrate how an early modern stereotype of madness has maintained continuity within a popular song tradition whilst undergoing cultural change

Implementing a resource list management system in an academic library

Purpose – The purpose of this paper is to review the key components of the introduction of a new resource list management system (RLMS) at Nottingham Trent University (NTU) using the Aspire application from Talis Education. It explains the key service goals; the implementation milestones; the main technical challenges which needed to be addressed; and the dynamic relationship between the rollout of the RLMS and existing selection, acquisition and resource delivery processes

Immobilisation of enzymes to Perloza cellulose resin : this thesis was presented in partial fulfilment of the requirements for the degree of Master of Science in Biochemistry at Massey University /

The studies reported in this thesis describe the use of Perloza™ beaded cellulose resin as a solid support for enzyme immobilisation via covalent binding. The aim of the project was to extend the uses for Perloza™ and to compare the use of well known solid support activation chemistries with a recently developed one for Perloza™. Preparations such as these have potential industrial uses. Three attachment chemistries were studied. The first activation employed 1,1-carbodiimidazole (CDI) then direct attachment of enzyme. The second again used CDI activation followed by attachment of a 6-aminocaproic acid spacer arm and then the enzyme. The final method used was attachment of a diol and subsequent oxidation to an aldehyde. The diol/aldehyde method had the advantage over the CDI methods of being based on aqueous chemistries. The two CDI based methods require extensive use of dry organic solvents. The enzymes investigated in this study were trypsin, chymotrypsin. α-amylase, horseradish peroxidase (HRPO) and alcohol dehydrogenase (ADH). Trypsin was immobilised successtully by all three chemistries. All preparations retained significant activity after immobilisation at room temperature as judged by the chromogenic substrate specific for trypsin N-α-benzoyl-DL-arginine-p-nitroanilide.HC1 (BAPNA). Measurable activity was retained in different studies from between 2 to 7 days at 60°C. The activity of immobilised trypsin with a synthetic peptide substrate was comparable to the activity of free trypsin with the same substrate. Chymotrypsin was also successfully immobilised using all three chemistries. Each preparation showed significant retention of activity after immobilisation as judged by the chromogentic substrate N-glutaryl-L.-phenylalanine-p-nitroanilide (GAPNA). Stabilisation to heating at 60°C was less successful than with trypsin but significant activity was still retained for between 3 and 6 hours. The activity of immobilised preparations with a peptide substrate was comparable to free chymotrypsin. α-Amylase, horseradish peroxidase and alcohol dehydrogenase were studied less extensively than trypsin and chymotrypsin. Nevertheless all three enzymes were successfully immobilised onto Perloza™-CDI-ACA and Perloza™-Diol/Aldehyde. Difficulty was encountered in achieving significant levels of any enzyme immobilisation to Perloza™-CDI for all three enzymes. Subsequent activity assays showed HRPO and α-amylase retained significant activity on all three resin preparations. ADH showed no measurable activity on Perloza™-CDI and very little activity on Perloza™- CDI-ACA and Perloza™-Diol/Aldehyde. Investigations have shown that enzymes can be immobilised on Perloza™ with retention of significant amounts of normal activity at room temperature and improved stability compared with free enzyme at high temperature. Comparisons of the CDI activations with the diol/aldeyde chemistry showed better performance by the latter in trypsin immobilisation and similar performance for chymotrypsin immobilisation. Horseradish peroxidase and ™-amylase were successfully immobilised using CDI/ACA and diol/aldehyde chemistries with the CDI/ACA giving higher initial specific activities than the diol/aldehyde preparation. Alcohol dehydrogenase was also successfully immobilised but gave no measurable activity