Trends and transitions in the institutional environment for public and private science

The last quarter-century bore witness to a sea change in academic involvement with commerce. Widespread university-based efforts to identify, manage, and market intellectual property (IP) have accompanied broad shifts in the relationship between academic and proprietary approaches to the dissemination and use of science and engineering research. Such transformations are indicators of institutional changes at work in the environment faced by universities. This paper draws upon a fifteen-year panel (1981–1995) of university-level data for 87 research-intensive US campuses in order to document trends and transitions in relationships among multiple indicators of academic and commercial engagement. The institutional environment for public and private science is volatile, shifting in fits and starts from a situation conducive to organizational learning through high volume patenting to a more challenging arrangement that links indiscriminate pursuit of IP with declines in both the volume and impact of academic science. The pattern and timing of these transitions may support an enduring system of stratification that offers increasing returns to first-movers while limiting the opportunities available to universities that are later entrants to the commercial realm. Unpacking the systematic effects of university research commercialization requires focused attention on the sources and trajectories of profound institutional change.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/42839/1/10734_2004_Article_2916.pd

The Properties and Functions of Alanopine Dehydogenase and Octopine Dehydrogenase from the Pedal Retractor Muscle of Strombidae (Class Gastropoda)

The pedal retractor muscles of Strombidae contain high activities of both alanopine dehydrogenase and octopine dehydrogenase, raising questions as to the functions of these two enzymes during muscle anoxia associated with locomotion. Alanopine dehydrogenase and octopine dehydrogenase were isolated from the pedal retractor muscle of Strombus luhuanus, and their structural and kinetic properties investigated. Alanopine dehydrogenase occurs as a single electrophoretic form with a molecular weight of approx. 42,000. Octopine dehydrogenase was electrophoretically polymorphic, existing as three alleles in the population of animals studied. The major form of the enzyme had a molecular weight of approx. 39,000. Both enzymes displayed similar pH optima for the forward (pyruvate reduction) reaction and similar Km values for the common substrates pyruvate and NADH. During bursts of leaping, both octopine and strombine/alanopine accumulated in the pedal retractor muscles of Strombidae. However, during recovery from exercise, only strombine/alanopine accumulated. Octopine was a potent inhibitor of the forward reaction catalyzed by octopine dehydrogenase, and may act to prevent further octopine production during the recovery phase. The results of this study show that both alanopine dehydrogenase and octopine dehydrogenase are functioning to catalyze the terminal step of anaerobic glycolysis during muscle anoxia associated with locomotion

Development of advanced NO sub x control concepts for coal-fired utility boilers

Hybrid technologies for reduction of NO{sub x} emissions from coal fired utility boilers may offer greater levels of NO{sub x} control than the sum of the individual technologies, leading to more cost effective emissions control strategies. Energy and Environmental Research Corporation had developed a hybrid NO{sub x} control strategy involving two proprietary concepts which has the potential to meet the US Department of Energy's goal at a significant reduction in cost compared to existing technology. The process has been named CombiNO{sub x}. CombiNO{sub x} is the integration of three separate NO control technologies: (1) Gas Reburning, (2) CO-Promoted Selective Non-Catalytic Reduction, and (3) Methanol Injection/NO{sub 2} Scrubbing

Evidence to the North Yorkshire Power Lines Inquiry

SIGLEAvailable from British Library Document Supply Centre- DSC:q94/24780 / BLDSC - British Library Document Supply CentreGBUnited Kingdo