NusG is an essential bacterial protein modulator of transcriptional elongation and termination events, and interacts directly with RNA polymerase and Rho protein. Found also in Archaea, NusG shows stretches of sequence similarity to the eukaryotic transcription elongation factor Spt5. Herein, the three-dimensional solution structure of the bacterial NusG from Thermus thermophilus, which shows 43% amino acid sequence similarity to the Escherichia coli NusG, is described, and a survey of NusG and Spt5 amino acid sequences is presented. Although there is a clear evolutionary and functional relationship between these proteins, it is evident from the structural, sequence, and biochemical data that their binding specificities to both nucleic acids and other proteins differ.

A new method, employing the mild oxidant N-bromosuccinimide, for the iodination of proteins for radioimmunoassay is described. Human prolactin, follicle-stimulating, luteinising, thyroid-stimulating, and growth hormones were iodinated with 125I by this method to specific activities up to 136 muCi/microgram. Incorporation of iodine ranged from 67% to 83% using 2 microgram hormone, 200 muCi Na125I, 0.5 nmol oxidant, and a reaction time of 15s. In comparative studies in immunological activity after iodination by this method was equal to, or greater than that by the chlorine gas, Iodo-Gen, or chloramine-T methods. The reagent is cheap and stable, and the method permits efficient use of antigen and iodide.

If you would like to write for this, or any other Emerald publication, then please use our Emerald for Authors service information about how to choose which publication to write for and submission guidelines are available for all. Please visit www.emeraldinsight.com/authors for more information. About Emerald www.emeraldinsight.comEmerald is a global publisher linking research and practice to the benefit of society. The company manages a portfolio of more than 290 journals and over 2,350 books and book series volumes, as well as providing an extensive range of online products and additional customer resources and services.Emerald is both COUNTER 4 and TRANSFER compliant. The organization is a partner of the Committee on Publication Ethics (COPE) and also works with Portico and the LOCKSS initiative for digital archive preservation. AbstractPurpose -The aim of this study is twofold: to evaluate empirically the incidence of co-creation activities; and to identify company characteristics that enable capabilities for innovation via co-creation. Design/methodology/approach -The study used a positivist research methodology that focused on data collection via a literature-based designed questionnaire, followed by analyses of the collected data. This first stage study focused investigation on a sample of high turnover companies, the "Top 250 Companies" annual list published by Durham University Business School, operating in the North East region of England. Eighty complete questionnaires were returned, representing a response rate of 32 per cent. Findings -The results of the survey indicated that co-creation activities and capabilities were not extensive in the sample population. However, the companies that were strategically focussed on meeting the demands of individual customers were more inclined to have developed capabilities necessary for co-creation activities. This finding supported the presuppositions for co-creation identified in the literature. There was also evidence in the survey that indicated the need for the greater use of information and computing technology in business processes in the sample population, and the improvement of communications systems to enhance co-creation activities and create value. Originality/value -This is the first attempt to explore and quantify co-creation activities in the UK across industry sectors, and to demonstrate how such analyses can be used to assist business growth and economic development.

No abstract

A CD4+ T cell epitope of the influenza virus matrix protein corresponding to the C terminus (QAYQKRMGVQMQRFK) was inserted into the VP7 gene of bluetongue virus (BTV). The chimeric protein was expressed by a dual recombinant Autographa californica polyhedrosis virus (AcNPV), which encodes the two inner capsid proteins VP3 and VP7 of BTV. When Spodoptera fRugiperda cells (Sf9 cells) were infected with this recombinant BTV, core-like particles (CLPs) were formed as demonstrated by electron microscopy. To study the immunogenicity of a foreign epitope deprived of its natural flanking sequences in vitro, purified CLPs expressing the T cell epitope were used to stimulate two different MHC class II-restricted CD4+ human T cell clones. One of these T cell clones, ALF 3.7 was specific for the inserted epitope, whereas the other T cell clone ALF 4.4 recognized shorter derivates of the given epitope. CLPs with the inserted epitope were presented as efficiently as purified influenza virus matrix protein to the clone ALF 3.7, whereas clone ALF 4.4 showed no proliferative response.