Literature DB >> 945746

Stereospecificity of lipases. Enzymatic hydrolysis of enantiomeric alkyldiacyl- and dialkylacylglycerols by lipoprotein lipase.

F Paltauf, E Wagner.   

Abstract

Lipoprotein lipase from dialyzed and lyophilized bovine skim milk hydrolyses specifically the ester in position 1 of triacylglycerols and of enantiomeric alkyldiacylglycerols. No such specificity could be observed when enantiomeric dialkylacylglycerols were used as substrates since hydrolysis in positions 1 and 3 occurred at the same rate. Dialkylacylglycerols are, therefore, unsuitable as model substrates for the assay of the stereospecificity of lipases.

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Year:  1976        PMID: 945746     DOI: 10.1016/0005-2760(76)90156-9

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  4 in total

Review 1.  Human pancreatic digestive enzymes.

Authors:  David C Whitcomb; Mark E Lowe
Journal:  Dig Dis Sci       Date:  2007-01-05       Impact factor: 3.199

2.  Studies on the substrate specificity of purified human milk lipoprotein lipase.

Authors:  C S Wang; A Kuksis; F Manganaro
Journal:  Lipids       Date:  1982-04       Impact factor: 1.880

3.  Use of a fluorescent radiolabeled triacylglycerol as a substrate for lipoprotein lipase and hepatic triglyceride lipase.

Authors:  N Dousset; A Negre; R Salvayre; P Rogalle; Q Q Dang; L Douste-Blazy
Journal:  Lipids       Date:  1988-06       Impact factor: 1.880

Review 4.  Determination of lipase specificity.

Authors:  R G Jensen; F A deJong; R M Clark
Journal:  Lipids       Date:  1983-03       Impact factor: 1.880

  4 in total

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