That T. Ngo
University of California, Irvine
30 Papers
433 Citations
That T. Ngo is an academic researcher from University of California, Irvine. The author has contributed to research in topics: Glucose oxidase & Immunoassay. The author has an hindex of 13, co-authored 30 publications.
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Papers
Enzyme-mediated immunoassay
That T. Ngo,Howard M. Lenhoff +1 more
- 01 Jan 1985
TL;DR: Separation-Free Enzyme Fluorescence Immunoassay by Continuous Flow Injection Analysis and Development of Immunochemical Enzyme Assays for Cardiac Isoenzymes.
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Spectrophotometric assay for ornithine decarboxylase
That T. Ngo,K. L. Brillhart,Rowland H. Davis,R. C. Wong,J. H. Bovaird,J. J. Digangi,Janet L. Ristow,J. L. Marsh,A. P. H. Phan,Howard M. Lenhoff +9 more
TL;DR: The three assays were found to be equivalent in sensitivity, with the spectrophotometric assay having the advantages of being relatively rapid, requiring only common laboratory equipment, and not requiring the use of radioactive isotopes.
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Recent advances in homogeneous and separation-free enzyme immunoassays.
That T. Ngo,Howard M. Lenhoff +1 more
TL;DR: The development of the versatile and sensitive analytical technique of quantitative radioimmunoassay (RIA) by Yalow and Berson in 1959 has revolutionized diagnostic methodology in clinical medicine and has provided a powerful analytical tool in biomedical research.
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Regulation of γ-aminobutyric acid synthesis in the vertebrate nervous system
Godfrey Tunnicliff,That T. Ngo +1 more
TL;DR: It is concluded that the overriding factors responsible for GAD regulation are not yet understood, but a possible mechanism relying on the direct feedback action of GABA on GAD activity has many attractive features.
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Kinetics of rat brain soluble catechol-O-methyltransferase and its inhibition by substrate analogues
Godfrey Tunnicliff,That T. Ngo +1 more
TL;DR: The initial rate and product inhibition patterns were consistent with an ordered BiBi mechanism and suggest that vanillic acid is the first product and S-adenosyl-L-homocysteine the second product to dissociate from the enzyme.
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