A new type of ultrasensitive bioluminogenic enzyme substrates. I. Enzyme substrates with D-luciferin as leaving group.
Biol Chem Hoppe Seyler
; 369(5): 407-11, 1988 May.
Article
en En
| MEDLINE
| ID: mdl-3166746
ABSTRACT
Derivatives of D-luciferin, D-luciferin methyl ester, D-luciferin O-sulfate, D-luciferin O-phosphate, D-luciferyl-L-N alpha-arginine and D-luciferyl-L-phenylalanine were used as highly sensitive substrates for carboxylic esterase, arylsulfatase, alkaline phosphatase and carboxypeptidases A, B and N. Enzymatic cleavage of the compounds by enzymes leading to the release of D-luciferin was demonstrated. Kinetic constants have been determined for D-luciferin methyl ester and carboxylic esterase, for D-luciferin O-sulfate and arylsulfatase, for D-luciferin O-phosphate and alkaline phosphatase, for D-luciferyl-L-phenylalanine and carboxypeptidase A, and for carboxypeptidases B and N and D-luciferyl-L-N alpha-arginine. All compounds proved to be highly sensitive substrates for the respective enzymes, permitting a limit of detection for enzymes between 10 and 500 fg per assay.
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Bases de datos:
MEDLINE
Asunto principal:
Arilsulfatasas
/
Sulfatasas
/
Hidrolasas de Éster Carboxílico
/
Carboxipeptidasas
/
Luciferina de Luciérnaga
/
Fosfatasa Alcalina
/
Luciferasas
Idioma:
En
Revista:
Biol Chem Hoppe Seyler
Asunto de la revista:
BIOQUIMICA
Año:
1988
Tipo del documento:
Article