Interlaboratory study into the proficiency of attribution of human serum butyrylcholinesterase phenotypes: Reference values of activities and inhibitor numbers

Acta Pharmaceutica

Volumn 51, Issue 4, 2001, Pages 289-296

  Simeon Rudolf, Vera ^a   Evans, Robert T ^a  

^a INSTITUTE FOR MEDICAL RESEARCH AND OCCUPATIONAL HEALTH   (Croatia)

Author keywords

Activity measurement; Butyrylcholinesterase; Butyrylcholinesterase phenotyping; Inhibition by dibucaine; Performance evaluation; Quality control; Reference values of activities and inhibitor numbers; Sodium fluoride and Ro 02 0683

Indexed keywords

CHOLINESTERASE INHIBITOR; CINCHOCAINE; FLUORIDE SODIUM;

ARTICLE; ENZYME ACTIVITY; ENZYME DEGRADATION; HUMAN; MAJOR CLINICAL STUDY; MUSCLE RELAXATION; PHENOTYPE; QUALITY CONTROL; REFERENCE VALUE;

EID: 0035701342     PISSN: 13300075     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (12)

1. Cholinesterase phenotyping: Clinical aspects and laboratory applications
2. Cholinesterase
3. Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine
4. The DNA mutation associated with the human butyrylcholinesterase K-variant and its linkage to the atypical variant mutation and other polymorphic sites
5. Laboratory study of the proficiency of cholinesterase phenotyping
6. Improved accuracy of cholinesterase phenotyping after participation in the proficieny survey
7. A method for the detection of atypical forms of human serum cholinesterase; determination of dibucaine numbers
8. A new and rapid colorimetric determination of acetylcholinesterase activity
9. Cholinesterase phenotyping and distribution of activity in sera of 346 individuals
10. An explanation for the different inhibitory characteristics of human serum butyrylcholinesterase phenotypes deriving from inhibition of atypical heterozygotes
11. Human serum cholineterase phenotypes: Reproducibility of inhibitor numbers and activity measurements
12. Value of butyrylthiocholine assay for identification of cholinesterase variants