Title : Lipoprotein lipase-catalyzed hydrolysis of phosphatidylcholine of guinea pig very low density lipoproteins and discoidal complexes of phospholipid and apolipoprotein: effect of apolipoprotein C-II on the catalytic mechanism.

Pub. Date : 1983 Jun

PMID : 6688442






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 To elucidate the mechanism by which apolipoprotein C-II (apoC-II) enhances the activity of lipoprotein lipase (LpL), discoidal phospholipid complexes were prepared with apoC-III and di[(14)C]palmitoyl phosphatidylcholine (DPPC) and containing various amounts of apoC-II. 1,2-Dipalmitoylphosphatidylcholine apolipoprotein C-II Cavia porcellus
2 To elucidate the mechanism by which apolipoprotein C-II (apoC-II) enhances the activity of lipoprotein lipase (LpL), discoidal phospholipid complexes were prepared with apoC-III and di[(14)C]palmitoyl phosphatidylcholine (DPPC) and containing various amounts of apoC-II. 1,2-Dipalmitoylphosphatidylcholine apolipoprotein C-II Cavia porcellus
3 The effect of apoC-II on enzyme kinetic parameters for LpL-catalyzed hydrolysis of DPPC complexes was compared to that on the parameters for hydrolysis of DPPC and trioleoylglycerol incorporated into guinea pig very low density lipoproteins (VLDL(p)) which lack the equivalent of human apoC-II. 1,2-Dipalmitoylphosphatidylcholine apolipoprotein C-II Cavia porcellus
4 In the presence of apoC-II, the V(max) for DPPC hydrolysis in guinea pig VLDL(p) increased at both pH 7.4 and pH 8.5 (2.4- and 3.2-fold, respectively); the value of K(m) did not change at either pH (0.23 mm). 1,2-Dipalmitoylphosphatidylcholine apolipoprotein C-II Cavia porcellus