Biomedical subjects

I Leesong

Publications and source records attributed to I Leesong.

3 recordsLinked to original sources

PubMed1996

Moving boundary electrophoretically mediated microanalysis.

Moving boundary sample introduction is described as an alternative to zonal injection methods for the electrophoretically mediated microanalysis (EMMA) of leucine aminopeptidase (LAP). The capillary was initially filled with the analyte solution while the faster-migrating substrate, L-leucine-p-nitroanilide, was maintained in the inlet reservoir. Upon application of an electric field, electrophoretic merging of the reagents proceeded, and the detectable reaction product, p-nitroaniline, was transported to the detector. The area, maximum height, inclining slope, and declining slope of the resulting triangular product profile were each directly proportional to the activity of LAP, and the observed migration times of the product profile features defined the volume and time of the incubation. The moving boundary technique offered more than an order of magnitude greater concentration sensitivity than the zonal injection EMMA method. This heightened sensitivity facilitated rapid analysis as the use of elevated electric field strenghts and short capillaries allowed for a 24-s kinetic determination of LAP.

Animals↗

PubMed1994

Selectivity in electrophoretically mediated microanalysis by control of product detection time.

Differential electrophoretic mobility between an analyte and its product offers electrophoretically mediated microanalysis (EMMA) a unique capability to selectively control the detection time of the product of a reaction-based chemical analysis. If an analyte and its product differ in migration velocity under the influence of an applied electric field, the apparent velocity and, consequently, the detection time of the product are dependent upon the relative amounts of time the product effectively traverses the capillary with the respective mobilities of the analyte and the product. Consequently, by controlling when the analytical reaction is allowed to occur, the detection time of the reaction product can be selectively maneuvered within a time window defined by the mobilities of the analyte and the product. This paper describes the use of this technique to manipulate the detection time of product profiles independently of nonreacting matrix interferants for the determination of both enzymes and substrates by EMMA. Furthermore, the ability to manipulate product detection times allows for simultaneous EMMA determinations of multiple enzymes or substrates.

Alcohol Dehydrogenase↗

PubMed1993

Electrophoretically mediated microanalysis of leucine aminopeptidase in complex matrices using time-resolved laser-induced fluorescence detection.

Leucine aminopeptidase, a clinically significant enzyme, was assayed in complex biological samples using a new technique termed electrophoretically mediated microanalysis. The assay was performed in capillary electrophoresis columns using time-resolved laser-induced fluorescence detection. Human serum, human urine, and Escherichia coli supernatant samples were assayed using this method. Results for serum and urine were within the ranges of expected values found in the literature. A low concentration of 6 x 10(-13) M enzyme in buffer was detected using this method. A detection limit (3 sigma) of 400 enzyme molecules in buffer was determined.

Buffers↗