Structure of human serum cholinesterase

Research output: Contribution to journalReview article

42 Scopus citations

Abstract

Human cholinesterase has recently been sequenced and cloned. It is a glycoprotein of 4 identical subunits, each subunit containing 9 carbohydrate chains and 3.5 disulfide bonds. Protein folding is likely to be very similar in human cholinesterase and Torpedo acetylcholinesterase. The cholinesterases have no significant sequence homology with the serine proteases and seem to belong to a separate serine esterase family.

Original languageEnglish (US)
Pages (from-to)125-128
Number of pages4
JournalBioEssays
Volume9
Issue number4
DOIs
StatePublished - Oct 1988
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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