Document Detail


A spectrophotometric assay for lipase activity utilizing immobilized triacylglycerols.
MedLine Citation:
PMID:  1779096     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
New substrates for the determination of lipase activity have been developed. Triacylglycerols were immobilized by adsorption on an appropriate carrier or adsorbent yielding a lipase substrate in a powder form. The adsorbed triacylglycerols were easily hydrolyzed by lipases present in a reaction mixture. The released fatty acids were extracted with benzene and converted to the corresponding Cu (II) salts (copper soaps) which were measured spectrophotometrically.
Authors:
I Safarík
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of biochemical and biophysical methods     Volume:  23     ISSN:  0165-022X     ISO Abbreviation:  J. Biochem. Biophys. Methods     Publication Date:    1991 Oct-Nov
Date Detail:
Created Date:  1992-03-10     Completed Date:  1992-03-10     Revised Date:  2000-12-18    
Medline Journal Info:
Nlm Unique ID:  7907378     Medline TA:  J Biochem Biophys Methods     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  249-53     Citation Subset:  IM    
Affiliation:
Laboratory of Analytical Chemistry, South Bohemian Biological Centre, Branisovská, Ceské Budĕjovice, Czechoslovakia.
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MeSH Terms
Descriptor/Qualifier:
Adsorption
Candida / enzymology
Lipase / metabolism*
Spectrophotometry*
Triglycerides / metabolism*
Chemical
Reg. No./Substance:
0/Triglycerides; EC 3.1.1.3/Lipase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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