Structure of human serum cholinesterase

descriptionPublicationkeyboard_double_arrow_right Article 01 Oct 1988 United States English Publisher:WileyJournal:BioEssays, volume 9, pages 125-128 (issn: 0265-9247, eissn: 1521-1878,

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Authors: Lockridge, Oksana;

doi: 10.1002/bies.950090406

pmid: 3067729

handle: 2027.42/50189

Structure of human serum cholinesterase

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Abstract

AbstractHuman 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.

Country

United States

Related Organizations

University of Michigan–Flint
United States
University of Michigan–Ann Arbor
United States
University of Michigan
United States

Keywords

Binding Sites, Macromolecular Substances, Science, Ecology and Evolutionary Biology, Molecular Sequence Data, Cell & Developmental Biology, Molecular, Natural Resources and Environment, Life and Medical Sciences, Health Sciences, Cholinesterases, Humans, Amino Acid Sequence, Cellular and Developmental Biology

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