Literature DB >> 8291677

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

K J Miller1, I Leesong, J Bao, F E Regnier, F E Lytle.   

Abstract

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.

Entities:  

Mesh:

Substances:

Year:  1993        PMID: 8291677     DOI: 10.1021/ac00070a017

Source DB:  PubMed          Journal:  Anal Chem        ISSN: 0003-2700            Impact factor:   6.986


  2 in total

1.  Increasing the efficiency of in-capillary electrophoretically mediated microanalysis reactions via rapid polarity switching.

Authors:  Brandi D Sanders; Rachel L Slotcavage; Diana L Scheerbaum; Christopher J Kochansky; Timothy G Strein
Journal:  Anal Chem       Date:  2005-04-15       Impact factor: 6.986

2.  N-Benzoyl leucomethylene blue as a novel substrate for the assays of horseradish peroxidase by spectrophotometry and capillary electrophoresis-laser-induced fluorometry.

Authors:  Jianchao Ren; Takashi Kaneta
Journal:  Anal Sci       Date:  2022-02-25       Impact factor: 2.081

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.