Immunological comparison of the usual and atypical human serum cholinesterase phenotypes

Harry W. Eckerson, Allen Oseroff, Oksana Lockridge, Bert N. La Du

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


Antiserum prepared against highly purified usual human serum cholinesterase (the most common phenotype) cross-reacted identically with the atypical serum cholinesterase. The level of circulating atypical enzyme protein, determined immunologically, was about 30% lower when the enzyme came from an atypical rather than a usual phenotype, and the level of enzyme activity measured enzymatically at Vmax with either o-nitrophenylbutyrate or benzoylcholine as substrate showed approximately the same degree of reduction. The average specific activity (activity at Vmax per microgram of enzyme protein) in sera from 28 usual and 20 atypical individuals did not differ significantly. These findings suggest that the atypical enzyme not only has altered catalytic properties (K)mbut also might be synthesized more slowly, or cleared in vivo more rapidly, than the usual enzyme.

Original languageEnglish (US)
Pages (from-to)93-108
Number of pages16
JournalBiochemical Genetics
Issue number1-2
StatePublished - Feb 1983
Externally publishedYes


  • atypical cholinesterase
  • cholinesterase
  • human esterase
  • quantitive enzyme variation

ASJC Scopus subject areas

  • Genetics
  • Ecology, Evolution, Behavior and Systematics
  • Molecular Biology
  • Biochemistry


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