Learning from Practice: How East Lancashire Hospitals' Pharmacy Service Has Embraced Information Technology.

The ethos of the pharmacy service at East Lancashire Hospitals NHS Trust (ELHT) could be described as 'let's make things better'. We have a history of innovation involving technology and people; one without the other does not work but together they are synergistic. The Trust currently does not have an electronic patient record (ePR) or electronic prescribing and medicines administration (ePMA), although we do have electronic prescribing for chemotherapy.

Life satisfaction and musculoskeletal complaints in a population seeking osteopathy care: consecutive sample of 611 patients.

Background: Life satisfaction is a component of the subjective well-being construct. Research consistently suggests that life satisfaction is associated with enhanced social benefits and improved health outcomes. However, its relationship to musculoskeletal health outcomes is underexplored.

Mining Xanthomonas and Streptomyces genomes for new pectinase-encoding sequences and their heterologous expression in Escherichia coli.

Microbial genome sequencing has left a legacy of annotated yet uncharacterized genes or open reading frames, activities that may have useful applications in health and/or the environment. We are interested in the discovery and characterization of potentially new pectinolytic activities for the enzymatic retting of natural bast fibers such as hemp and flax. A highlight in this study is the discovery of a cold-active pectate lyase among five pectate-lyase-encoding sequences and two polygalacturonase-encoding sequences that we have cloned from the genomes of Xanthomonas campestris pv.

The dodecameric vanadium-dependent haloperoxidase from the marine algae Corallina officinalis: cloning, expression, and refolding of the recombinant enzyme.

The dodecameric vanadium-dependent bromoperoxidase from Corallina officinalis has been cloned and over-expressed in Escherichia coli. However, the enzyme was found to be predominantly in the form of inclusion bodies. This protein presents a challenging target for refolding, both due to the size (768kDa) and quaternary structure (12x64kDa).