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Differences in reactivity of four butyrylcholinesterase isozymes towards substrate and inhibitors
- Source :
- Biochemical and biophysical research communications. 46(1)
- Publication Year :
- 1972
-
Abstract
- Four isozymes of horse serum butyrylcholinesterase have been resolved by means of polyacrylamide gel electrophoresis combined with specific substrate staining and gel-scanning procedures. They differ 5-fold in their Km for butyrylthiocholine and 5 and 7-fold in reactivity with two organophosphates, malaoxon and Tetram.
- Subjects :
- Electrophoresis
Insecticides
Chemical Phenomena
Biophysics
Sulfides
Biochemistry
Isozyme
Butyrylthiocholine
Choline
chemistry.chemical_compound
Malaoxon
Animals
Cholinesterases
Reactivity (chemistry)
Trypsin
Horses
Molecular Biology
Polyacrylamide gel electrophoresis
Butyrylcholinesterase
Cholinesterase
Acrylamides
biology
Substrate (chemistry)
Organothiophosphorus Compounds
Cell Biology
Molecular biology
Isoenzymes
Butyrates
Chemistry
Kinetics
chemistry
biology.protein
Cholinesterase Inhibitors
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 46
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications
- Accession number :
- edsair.doi.dedup.....1160f2857ad743e6e7759c403b9ba44a