Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving hydrolase
Patent
1993-01-13
1995-08-29
Beisner, William H.
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving hydrolase
435 77, 435 28, 435810, 435975, 536 2625, C12Q 134, C12Q 128, C07H 1906
Patent
active
054459427
ABSTRACT:
Hydrolase enzymes are sensitively determined using novel substituted FAD substrates. The substituted FAD substrates are hydrolysed to FAD by the enzyme to be detected. The FAD is then combined with an apoenzyme to form a holoenzyme which is used to initiate a reaction that leads to a detectable product. When the hydrolase to be detected is phosphatase, the novel substrate is a phosphorylated derivative of FAD. A suitable apoenzyme is apo-glucose oxidase which provides exceptional sensitivity. Apo-D-amino acid oxidase, which is suitable for use in a "single pot" assay system, can also be used.
REFERENCES:
patent: 4318982 (1982-03-01), Hornby et al.
patent: 4318983 (1982-03-01), Hornby et al.
Methods in Enzymology, vol. 122 pp. 185-192 Decker, K., "Luminometric Determination of Fad" (1986).
Daniel et al. Chem Abs. 98 158456y (1983) "Hydrolysis of FMN and FAD by alkaline phosphatase of the intestinal brush-border membrane".
Chemical Abstracts, vol. 98, No. 19, 9 May 1983 (Columbus, Ohio, US), H. Daniel et al.: "Hydrolysis of FMN and FAD by alkaline phosphatase of the intestinal brush-border membrane".
Eggelte Hendrikus J.
Harbron Stuart
Hollaway, deceased Michael R.
Holloway, legal representative Ann
Rabin Brian R.
Beisner William H.
Brunelle Jan P.
Dreger Walter H.
Gitomer Ralph
London Biotechnology Limited
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