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.
Miller
K J
KJ
Department of Chemistry, Purdue University, West Lafayette, Indiana 47907-1393.
Leesong
I
I
Bao
J
J
Regnier
F E
FE
Lytle
F E
FE
D002021:Buffers; D004586:Electrophoresis; D004926:Escherichia coli / Q000201:enzymology*; D005453:Fluorescence; D006801:Humans; D007931:Leucyl Aminopeptidase / Q000032:analysis* / Q000097:blood / Q000652:urine; D012015:Reference Standards
D002021:Buffers; D007931:Leucyl Aminopeptidase