Triglyceride lipase activities in rat liver.
A kinetic study of neutral and alkaline triglyceride lipase activities from different liver homogenate fractions is reported. Lipase activities are studied with triolein as substrate and are determined by quantification of the released oleic acid liberated. Heparin-releasable, microsomal and mitochondrial lipase activities are studied as a function of time, protein concentration and substrate concentration. The neutral triglyceride lipase associated with mitochondrial membranes is kinetically different from the alkaline lipase, localized on the plasma membrane, which probably contaminates microsomal and soluble fractions.
Rodríguez-Fernández
C
C
Department of Biochemistry, Faculty of Science, University of the Basque Country, Bilbao, Spain.
Ruiz-Larrea
M F
MF
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008049:Lipase / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology; D051381:Rats; D011919:Rats, Inbred Strains
D007527:Isoenzymes; D008049:Lipase