A New Ultrasensitive Bioluminogenic Enzyme Substrate forβ-Galactosidase
- 1 January 1992
- journal article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 373 (2) , 1187-1192
- https://doi.org/10.1515/bchm3.1992.373.2.1187
Abstract
A derivative of D-luciferin, D-luciferin-O-beta-galactoside, was synthesized and used as highly sensitive substrate for beta-galactosidase. The substrate was physicochemically characterized. Enzymatic cleavage of the new compound by beta-galactosidase was demonstrated and kinetic constants Km, Vmax, kcat and kcat/Km have been determined. The compound has been proved to be a highly sensitive substrate for beta-galactosidase, permitting a limit of detection of 3.7 x 10(-19) mol of enzyme per assay.Keywords
This publication has 4 references indexed in Scilit:
- New, bioluminescence-enhanced detection systems for use in enzyme activity tests, enzyme immunoassays, protein blotting and nucleic acid hybridizationMolecular and Cellular Probes, 1989
- New, sensitive, radioactive-free bioluminescence-enhanced detection system in protein blotting and nucleic acid hybridizationJournal of Bioluminescence and Chemiluminescence, 1989
- A New Type of Ultrasensitive Bioluminogenic Enzyme Substrates. I. Enzyme Substrates with D-Luciferin as Leaving GroupBiological Chemistry Hoppe-Seyler, 1987
- The Structure and Synthesis of Firefly LuciferinJournal of the American Chemical Society, 1963