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Cholinesterase bonded to paper

Authors :
F. X. Hasselberger
R. O. Stasiw
Harry D. Brown
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