SwePub - search: WFRF:(Eriksson Håkan)

Enumeration	Reference	Cover	Find
1.	Eriksson, Håkan, 1952- (author) Studies on the catalytic mechanism of butyrylcholinesterase and the development of a cholinesterase assay for clinical applications 1980 Doctoral thesis (other academic/artistic)abstract This investigation is concerned with the kinetic behaviour of butyrylcholinesterase and the development of a simple, fast and reliable method for the determination of cholinesterases in whole blood.Steady state kinetic studies with selective inhibitors and with a number of substrates at several different conditions were used in an attempt to explain the observed substrate activation of horse serum butyrylcholinesterase. Another approach used was ligand binding studies.A plausible catalytic mechanism involves binding of a substrate molecule to the acylated active site of the enzyme. This binding should increase the rate of hydrolysis of the acylated enzyme.The spectrophotometric assay developed for cholinesterases discriminates between the two cholinesterases in blood. It also yields reliable estimates of cholinesterase activities from whole blood of individuals exposed to anti-cholinesterases.

Eriksson, Håkan, 1952- (author)
Studies on the catalytic mechanism of butyrylcholinesterase and the development of a cholinesterase assay for clinical applications
1980
Doctoral thesis (other academic/artistic)abstract
- This investigation is concerned with the kinetic behaviour of butyrylcholinesterase and the development of a simple, fast and reliable method for the determination of cholinesterases in whole blood.Steady state kinetic studies with selective inhibitors and with a number of substrates at several different conditions were used in an attempt to explain the observed substrate activation of horse serum butyrylcholinesterase. Another approach used was ligand binding studies.A plausible catalytic mechanism involves binding of a substrate molecule to the acylated active site of the enzyme. This binding should increase the rate of hydrolysis of the acylated enzyme.The spectrophotometric assay developed for cholinesterases discriminates between the two cholinesterases in blood. It also yields reliable estimates of cholinesterase activities from whole blood of individuals exposed to anti-cholinesterases.

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