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Cholinesterase bonded to paper
- Source :
- Canadian journal of biochemistry. 48(12)
- Publication Year :
- 1970
-
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).
Details
- ISSN :
- 00084018
- Volume :
- 48
- Issue :
- 12
- Database :
- OpenAIRE
- Journal :
- Canadian journal of biochemistry
- Accession number :
- edsair.doi.dedup.....a2320fd451a1142e14c236a1bf3fdf66