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Clinical Chemistry 39: 224-228, 1993;
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Clinical Chemistry, Vol 39, 224-228, Copyright © 1993 by American Association for Clinical Chemistry

Modifying an enzyme immunoassay of immunoreactive trypsinogen to use time-resolved fluorescence

RG Ryall, EM Gjerde, RL Gerace and E Ranieri
Department of Chemical Pathology, Adelaide Children's Hospital, South Australia.

A coated microtiter-well, enzyme-linked immunometric assay for quantifying immunoreactive trypsinogen in dried blood spots was modified to use time-resolved fluorescence of europium in place of end- point enzymatic color development as the quantification step. The streptavidin-horseradish peroxidase and color development solutions supplied as packaged reagents were replaced by europium-labeled avidin, and the signal was developed with commercially available enhancement solution and read by time-resolved fluorescence. The change of label from enzyme to europium increased the dynamic range of the assay by about 5-fold, reduced the detection limit 10-fold, and halved the intra- and interassay imprecision. The improved analytical precision and stability of the modified assay resulted in a more precise description of the population distribution of immunoreactive trypsinogen values in newborns, showing less variance in the upper centiles. This effect is of paramount importance when using this assay for neonatal screening for cystic fibrosis.


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P. J. Meikle, D. A. Brooks, E. M. Ravenscroft, M. Yan, R. E. Williams, A. E. Jaunzems, T. K. Chataway, L. E. Karageorgos, R. C. Davey, C. D. Boulter, et al.
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 BMJHome page
E Ranieri, B D Lewis, R L Gerace, R G Ryall, C P Morris, P V Nelson, W F Carey, and E F Robertson
Neonatal screening for cystic fibrosis using immunoreactive trypsinogen and direct gene analysis: four years' experience
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[Abstract] [Full Text]


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