VLDL substrate properties and efficiency of their metabolic transformation by LPL.
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.
Dergunov
A D
AD
Department of Biochemistry, USSR Research Centre for Preventive Medicine, Moscow.
Shuvaev
V V
VV
Perova
N V
NV
D000818:Animals; D053304:Apolipoprotein C-II; D053305:Apolipoprotein C-III; D001056:Apolipoproteins C / Q000097:blood; D002417:Cattle; D005260:Female; D006801:Humans; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008079:Lipoproteins, VLDL / Q000097:blood*; D008892:Milk / Q000201:enzymology; D013379:Substrate Specificity
D053304:Apolipoprotein C-II; D053305:Apolipoprotein C-III; D001056:Apolipoproteins C; D008079:Lipoproteins, VLDL; D008071:Lipoprotein Lipase