1. Cholinesterase bonded to paper
- Author
-
F. X. Hasselberger, R. O. Stasiw, and Harry D. Brown
- Subjects
chemistry.chemical_classification ,Paper ,Chromatography ,Hot Temperature ,biology ,General Medicine ,Kinetics ,Enzyme ,chemistry ,Drug Stability ,Acetylcholine Chloride ,biology.protein ,Animals ,Cholinesterases ,Thermal stability ,Horses ,Cellulose ,Azo Compounds ,Lower activity ,Cholinesterase - Abstract
Cholinesterase has been bonded to Procion brilliant orange – DEAE-cellulose. The matrix-supported enzyme has a lower activity than the free enzyme in solution; thermal stability, however, is much greater. A marked difference in the Km (apparent) value of the derivatized protein was observed (substrate used was acetylcholine chloride, free Cholinesterase Km = 9.6 × 10−4 M, bound Cholinesterase Km = 1.0 × 10−2 M).
- Published
- 1970