Article
Mice expressing only covalent dimeric heparin binding-deficient lipoprotein lipase: muscles inefficiently secrete dimeric enzyme.
The Journal of biological chemistry - 2 Jan 2004
Lutz E Peer, Kako Yuko, Yagyu Hiroaki, Heeren Joerg, Marks Steven, Wright Thamrah, Melford Kristan, Ben-Zeev Osnat, Radner Herbert, Merkel Martin, Bensadoun André, Wong Howard, Goldberg Ira J
Abstract excerpt
Lipoprotein lipase (LpL) hydrolyzes triglycerides of circulating lipoproteins while bound as homodimers to endothelial cell surface heparan sulfate proteoglycans. This primarily occurs in the capillary beds of muscle and adipose tissue. By creating a mouse line that expresses covalent dimers of heparin-binding deficient LpL (hLpLHBM-Dimer) in muscle, we confirmed in vivo that linking two LpL monomers in a head to...
Topics
- Amino Acid Sequence
- Animals
- Binding Sites
- COS Cells
- Chlorocebus aethiops
- Cholesterol
- Chromatography, Affinity
- Dimerization
- Enzyme Stability
- Genotype
- Heparin
- Humans
- Kinetics