Article
In vitro expression and site-specific mutagenesis of the cloned human lipoprotein lipase gene. Potential N-linked glycosylation site asparagine 43 is important for both enzyme activity and secretion.
The Journal of biological chemistry - 5 Apr 1990
Semenkovich C F, Luo C C, Nakanishi M K, Chen S H, Smith L C, Chan L
Abstract excerpt
Detailed structure-function information about human lipoprotein lipase (LPL) is unavailable because it is difficult to purify large amounts of the enzyme for study. To circumvent this problem, we constructed an in vitro LPL expression vector. Human LPL cDNA was cloned and inserted into the expression vector p91023(B). After transfection of COS M-6 cells with the human LPL cDNA construct, LPL enzyme activity was...
Topics
- Amino Acid Sequence
- Apolipoprotein C-II
- Apolipoproteins C
- Asparagine
- Cell Line
- Cloning, Molecular
- DNA
- Gene Expression
- Genetic Vectors
- Glycosylation
