Structure of human serum cholinesterase

Research output: Contribution to journalReview article

40 Citations (Scopus)

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

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Cholinesterases
Serum
Protein folding
Torpedo
Protein Folding
Serine Proteases
Acetylcholinesterase
Sequence Homology
Disulfides
Glycoproteins
Carbohydrates

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Structure of human serum cholinesterase. / Lockridge, Oksana.

In: BioEssays, Vol. 9, No. 4, 10.1988, p. 125-128.

Research output: Contribution to journalReview article

Lockridge, Oksana. / Structure of human serum cholinesterase. In: BioEssays. 1988 ; Vol. 9, No. 4. pp. 125-128.
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