ELCA

One year before Ayres publications [7,8], Cornelissen [9] completed his PhD dissertation in which he had combined life cycle analysis with exergy analysis. He called this extension of LCA exergetic life cycle analysis. He explained that ELCA should be part of every LCA because the loss via dissipation of exergy is one of the most important parameters to properly assess a process and measure the depletion of natural resources. Cornelissen even went one step further and extended ELCA to what he called zero-emission ELCA. In this extension of ELCA, the exergy required for the abatement of emissions, that is, the removal and reuse of environmentally friendly storage of emissions, is accounted for. Cornelissen illustrated his ideas with examples of... 

Next, Cornelissen extended the LCA study to include the effect of depletion of natural resources making use of ELCA, the exergetic life cycle assessment. In this analysis a full mass and energy balance was made, that is, a first law analysis. Exergy values for all mass and energy streams were included in accordance with the Tables 6.1, 6.2, 6.3, 7.1, 7.2, 7.3 and 7.4 in Chapters 6 and 7. This analysis clearly showed where work was available in inputs and outputs and where it was lost. He could show that the cup scored less favorable than the mug in terms of depletion of natural resources (817 MJ vs. 442 MJ). 

Doellgast, G. J., TrLscott, M. X., Buss, D, H., and West, J. (1988). Extrinsic pathway enzyme-linked coagulation assay (EP-ELCA). Clin. Chetr. 34, 294-299. 

Quite recently, the structures of SERCA from rabbit hind leg muscle in the ElCa-state complexed with trinitrophenyl-AMP and two bound Ca2+-ions as well as of Ca- and... 

Figure 4. Schematic depiction of the ELCA used with permission of the authors and publisher (10).

Figure 5. Apparatus for incorporation of alkaline phosphatase into solid-phase fibrin in the ELCA. (A) Silicone rubber nubs. (B) Nubs inserted into microtiter plate wells. (Courtesy G.J. Doellgast and ELCATech).

Figure 6. Results of type A, B, and E botulism neurotoxin assays using the ELCA sensitivity and specificity for each type can be seen. Photograph from reference 10, used with permission of the authors and the publisher.

This method has been modified more recently using a solution-phase complexing of the toxin to either biotin-labeled antitoxin or chicken antitoxin prior to binding of the complex to the solid-phase plate (9). Doellgast et al. (11) have also devised an adaptation of the ELISA/ELCA for detecting human antibodies to botulism toxins types A, B, and E. 

The sensitivity of the early ELISA methods (51) was in the same range as previous in vitro methods, but increased greatly with the incorporation of amplifier systems (58,64). Specificity has also improved with the preparation of antitoxins against highly purified toxins and use of monoclonal antibodies (64). The reports on the ELCA method describe meticulous preparation of high quality reagents and an exceptionally effective amplification which utilizes the Russell s viper venom factor X activator to initiate the clotting cascade (9,10). Its sensitivity appears to equal or exceed that of the mouse. 

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