Bile salt activation of human cholesterol esterase does not require protein dimerisation.

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dc.contributor.author Loomes, KM
dc.contributor.author Senior, HE
dc.coverage.spatial England
dc.date.accessioned 2022-06-23T04:35:35Z
dc.date.available 2022-06-23T04:35:35Z
dc.date.issued 1997-04
dc.identifier.citation (1997). FEBS Letters, 405(3), 369-372.
dc.identifier.issn 0014-5793
dc.identifier.uri https://hdl.handle.net/2292/60120
dc.description.abstract Human milk cholesterol esterase (bile salt-activated lipase) plays a role in the dietary uptake of triacylglyceride and cholesteryl ester. The activities toward these substrates are mediated through a unique bile salt-activated mechanism. Previously, it has been proposed that a necessary step in this process is prior protein dimerisation in the presence of primary bile salts. In this study, we addressed the role of protein dimerisation by investigating bile salt interactions on full length and truncated recombinant forms, as analysed by size exclusion chromatography and concanavalin A Sepharose binding experiments. The present findings demonstrate that protein dimerisation is not an obligatory component of the bile salt-activated pathway. A new functional role for the glycosylated C-terminal domain in cholesterol esterase is also demonstrated in the prevention of non-specific hydrophobic interactions.
dc.format.medium Print
dc.language eng
dc.publisher Wiley
dc.relation.ispartofseries FEBS letters
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher.
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm
dc.subject Humans
dc.subject Salts
dc.subject Bile Acids and Salts
dc.subject Macromolecular Substances
dc.subject Glycoproteins
dc.subject Recombinant Proteins
dc.subject Enzyme Activation
dc.subject Protein Binding
dc.subject Structure-Activity Relationship
dc.subject Sterol Esterase
dc.subject Nutrition
dc.subject Digestive Diseases
dc.subject Prevention
dc.subject 2.1 Biological and endogenous factors
dc.subject Science & Technology
dc.subject Life Sciences & Biomedicine
dc.subject Biochemistry & Molecular Biology
dc.subject Biophysics
dc.subject Cell Biology
dc.subject cholesterol esterase
dc.subject lysophospholipase
dc.subject carboxylester lipase
dc.subject bile salt activation
dc.subject bile salt-stimulated lipase
dc.subject PROLINE-RICH REPEATS
dc.subject HUMAN-MILK
dc.subject STIMULATED LIPASE
dc.subject CANDIDA-CYLINDRACEA
dc.subject INTERFACIAL ACTIVATION
dc.subject HYDROLASE
dc.subject GLYCOSYLATION
dc.subject CONFORMATION
dc.subject SUBSTRATE
dc.subject IDENTITY
dc.subject 0601 Biochemistry and Cell Biology
dc.subject Biomedical
dc.subject 0304 Medicinal and Biomolecular Chemistry
dc.subject 0603 Evolutionary Biology
dc.title Bile salt activation of human cholesterol esterase does not require protein dimerisation.
dc.type Journal Article
dc.identifier.doi 10.1016/s0014-5793(97)00215-9
pubs.issue 3
pubs.begin-page 369
pubs.volume 405
dc.date.updated 2022-05-05T01:44:52Z
dc.rights.holder Copyright: The author en
dc.identifier.pmid 9108320 (pubmed)
pubs.author-url https://www.ncbi.nlm.nih.gov/pubmed/9108320
pubs.end-page 372
pubs.publication-status Published
dc.rights.accessrights http://purl.org/eprint/accessRights/RetrictedAccess en
pubs.subtype Research Support, Non-U.S. Gov't
pubs.subtype Journal Article
pubs.elements-id 45524
pubs.org-id Science
pubs.org-id Biological Sciences
pubs.org-id Science Research
pubs.org-id Maurice Wilkins Centre (2010-2014)
dc.identifier.eissn 1873-3468
dc.identifier.pii S0014-5793(97)00215-9
pubs.record-created-at-source-date 2022-05-05
pubs.online-publication-date 1997-11-07


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