Back to Search
Start Over
Chromogenic substrate from 4-nitro-1-naphthol for hydrolytic enzyme of neutral or slightly acidic optimum pH: 4-Nitro-1-naphthyl-β-d-galactopyranoside as an example
- Source :
- Bioorganic & Medicinal Chemistry Letters. 23:646-649
- Publication Year :
- 2013
- Publisher :
- Elsevier BV, 2013.
-
Abstract
- At pH from 5.5 to 7.6, absorptivity of 4-nitro-1-naphthol at 450 nm is over 2.1-fold of that of para-nitrophenol at 405 nm and over 9.6-fold of that of ortho-nitrophenol at 415 nm. On 4-nitro-1-naphthyl-β-D-galactopyranoside at pH 7.4, catalytic efficiency of Escherichia coli β-D-galactosidase is 3-fold of that on para-nitrophenyl-β-D-galactopyranoside and about 40% of that on ortho-nitrophenyl-β-D-galactopyranoside, and produces a lower quantification limit of penicillin G by enzyme-linked-immunoabsorbent-assay. Hence, 4-nitro-1-naphthol is favorable to prepare chromogenic substrates of hydrolytic enzymes of neutral or slightly acidic optimum pH.
- Subjects :
- 1-Naphthol
Clinical Biochemistry
Inorganic chemistry
Pharmaceutical Science
Enzyme-Linked Immunosorbent Assay
Naphthols
Naphthalenes
medicine.disease_cause
Biochemistry
Nitrophenols
Hydrolysis
chemistry.chemical_compound
Glucosides
Drug Discovery
medicine
Molecule
Molecular Biology
Escherichia coli
chemistry.chemical_classification
Molecular Structure
Chromogenic
Organic Chemistry
Substrate (chemistry)
Penicillin G
Hydrogen-Ion Concentration
beta-Galactosidase
Enzyme
Chromogenic Compounds
chemistry
Nitro
Molecular Medicine
Nuclear chemistry
Subjects
Details
- ISSN :
- 0960894X
- Volume :
- 23
- Database :
- OpenAIRE
- Journal :
- Bioorganic & Medicinal Chemistry Letters
- Accession number :
- edsair.doi.dedup.....3846a965a334c717d169565de8da3bc7