These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: VLDL substrate properties and efficiency of their metabolic transformation by LPL. Author: Dergunov AD, Shuvaev VV, Perova NV. Journal: Experientia; 1989 May 15; 45(5):461-3. PubMed ID: 2721636. Abstract: A study was made of the regulation of the triglyceride hydrolysis catalysed by LPL from bovine milk, by the apoproteins from human plasma VLDL. Both isolated apolipoproteins, and those found on the surface of plasma VLDL particles, were investigated. A concentration-dependent activating action of apo C-II on the hydrolysis of emulsified triolein, and uncompetitive inhibition of VLDL triglyceride hydrolysis by apo C-III were found. It is suggested that VLDL lipolysis might be controlled in vivo through the variation of the relative surface content of these enzymatic activity modulators.[Abstract] [Full Text] [Related] [New Search]