Document Detail

Substrate specificity studies of partially purified rabbit heart lipoprotein lipase.
MedLine Citation:
PMID:  3178503     Owner:  NLM     Status:  MEDLINE    
Rabbit heart lipoprotein lipase (LPL) was partially purified by affinity chromatography. The purified enzyme was characterized by salt inhibition, the requirement of a serum co-factor and an alkaline pH optimum. Because of the known hypocholesterolemic effect of dietary polyunsaturated fat in this and other species, the fatty acyl substrate specificity of this lipase was also studied. Both saturated and unsaturated fatty acid chain hydrolysis were investigated using synacyl and mixed acyl triglyceride emulsion substrates. It was found that trans, monounsaturated and some saturated fatty acids were more favorably hydrolyzed than polyunsaturated cis fatty acids. Positional specificity was also observed. The physiological significance of these findings may relate to a) the production of lipoprotein remnant particles relatively enriched in polyunsaturated fatty acids, especially when consumed in the diet and b) the subsequent preferential delivery of these fatty acids to the liver.
J E Bauer
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Artery     Volume:  15     ISSN:  0098-6127     ISO Abbreviation:  Artery     Publication Date:  1988  
Date Detail:
Created Date:  1988-11-17     Completed Date:  1988-11-17     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  7508494     Medline TA:  Artery     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  272-91     Citation Subset:  IM    
Department of Physiological Sciences, J.H. Miller Health Sciences Center, University of Florida, Gainesville 32610.
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MeSH Terms
Chromatography, Affinity
Hydrogen-Ion Concentration
Lipoprotein Lipase / metabolism*
Myocardium / enzymology*
Substrate Specificity
Grant Support
Reg. No./Substance:
EC Lipase

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