| Phosphatidylcholine substrate specificity of lecithin:cholesterol acyltransferase. | |
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MedLine Citation:
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PMID: 746344 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Lecithin:cholesterol acyltransferase (LCAT) has been partially purified by the combined method of ultracentrifugation and dextranblue-2000 4 B affinity chromatography. The enzyme was incubated with liposomes consisting of phosphatidylcholine-cholesterol in a molar ratio of 10/1. Chemically synthesized phosphatidylcholine substrates with labeled fatty acids in 1-and 2-position were chosen to evaluate the degree of transesterification. It was found that the fatty acid in the 1-position of phosphatidylcholine significantly influences cholesteryl ester formation, both by its direct involvement in the LCAT reaction and its contribution to the physico-chemical properties of phosphatidylcholine. |
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Authors:
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G Assmann; G Schmitz; N Donath; D Lekim |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Scandinavian journal of clinical and laboratory investigation. Supplementum Volume: 150 ISSN: 0085-591X ISO Abbreviation: Scand. J. Clin. Lab. Invest. Suppl. Publication Date: 1978 |
Date Detail:
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Created Date: 1979-05-23 Completed Date: 1979-05-23 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 2984789R Medline TA: Scand J Clin Lab Invest Suppl Country: NORWAY |
Other Details:
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Languages: eng Pagination: 16-20 Citation Subset: IM |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Chemical Phenomena Chemistry Cholesterol Esters / analysis Fatty Acids / analysis Humans Molecular Conformation Phosphatidylcholine-Sterol O-Acyltransferase* / analysis, isolation & purification Phosphatidylcholines* / analysis, chemical synthesis* |
| Chemical | |
Reg. No./Substance:
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0/Cholesterol Esters; 0/Fatty Acids; 0/Phosphatidylcholines; EC 2.3.1.43/Phosphatidylcholine-Sterol O-Acyltransferase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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