Journal ArticleDOI
The action of normal and atypical cholinesterase of human serum upon a series of esters of choline
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The results of a comparison of the actions of individual human sera support evidence previously obtained for the existence of two different types of pseudocholinesterase in man.Abstract:
The results of a comparison of the actions of individual human sera support evidence previously obtained for the existence of two different types of pseudocholinesterase in man. Maximum rates of hydrolysis of choline esters by human sera containing the normal type of cholinesterase were two to four times greater than the maximum rates obtained with sera containing atypical esterase. Human sera with the normal type of cholinesterase hydrolyzed butyrylcholine at a considerably faster rate than pentanoylcholine; atypical esterase hydrolyzed pentanoylcholine at approximately the same rate as butyrylcholine. All Michaelis constants for the normal enzyme were lower than those for the atypical enzyme by a factor which varied from 1.4 to 6.4. The data were compatible with the assumption of a linear relationship between the log of the Michaelis constants and the number of acyl carbons in the choline esters, but the slopes differed significantly for the two enzymes. For a homologous series of choline esters, there ...read more
Citations
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Journal ArticleDOI
Plasma cholinesterase variants and the anaesthetist.
TL;DR: Biochemical properties of plasma cholinesterase of significance to the anaesthetist are reviewed and three new drugs are developed that target these properties.
Journal ArticleDOI
Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine.
TL;DR: Comparison of amino acid sequences of esterases and proteases shows that cholinesterase belongs to a new family of serine esterase which is different from the serine proteases.
Journal ArticleDOI
Average heterozygosity per locus in man: an estimate based on the incidence of enzyme polymorphisms
Harry Harris,D. A. Hopkinson +1 more
TL;DR: Data from electrophoretic surveys of enzymes in European populations are reviewed and three new models are proposed for the determinants of infectious disease in these populations.
Journal ArticleDOI
[A kinetic method for determination of the activity of pseudocholinesterase (acylcholine acyl-hydrolase 3.1.1.8.)].
TL;DR: The substrate butyrylthiocholineiodide reacts with pseudocholine esterase to yield thiocholine, which is able to reduce 5,5-dithiobis-2-nitrobenzoate to 5-mercapto-2 -nitro Benzoate, recognizable by its yellow colour.
Book ChapterDOI
The plasma cholinesteerases: a new perspective.
TL;DR: Recommendations for collecting and storing plasma and serum specimens and laboratory procedures used for distinguishing the more common serum cholinesterase variants are also discussed in the chapter.
References
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Journal ArticleDOI
The Determination of Enzyme Dissociation Constants
Hans Lineweaver,Dean Burk +1 more
TL;DR: On the basis of the assumed theory the rate of the observed reaction is directly proportional to the concentration of the enzyme-substrate compound, where (E:l = (ES).
Journal ArticleDOI
A Note on the Kinetics of Enzyme Action
TL;DR: The equation of Michaelis and Menten [1913] has been applied with success by Kuhn [1924] and others to numerous cases of enzyme action and it is desirable to examine its theoretical basis.
Journal ArticleDOI
Some statistical data on atypical cholinesterase of human serum
W. Kalow,D. R. Gunn +1 more
TL;DR: The occurrence of atypical serum cholinesterase (pseudocholinestersterase) was determined in a population which consisted of 2000 healthy persons and 2400 mental patients.
Journal ArticleDOI
The activity of various esterase inhibitors towards atypical human serum cholinesterase
Werner Kalow,R.O. Davies +1 more
TL;DR: The concept of the existence of a usual and of an atypical form of human serum cholinesterase was thereby supported and the shape of concentration-inhibition curves obtained with sera of the last-named category permitted no other interpretation than the presence of a mixture of two enzymes.
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