Article
Lys and fibrinogen binding of wild-type (Trp72) and mutant (Arg72) human apo(a) kringle IV-10 expressed in E coli and CHO cells.
Arteriosclerosis, thrombosis, and vascular biology - 1 Mar 1996
Klezovitch O, Scanu A M
Abstract excerpt
In a previous study, we identified a lysine (Lys)-binding-defective form of human lipoprotein(a) and attributed this defect to the presence of a Trp72-->Arg mutation in apolipoprotein(a) [apo(a)] kringle IV-10. To document this relationship, we expressed both wild-type (wt) and mutant (mut) forms...
Topics
- Amino Acid Sequence
- Animals
- Apolipoproteins
- Apoprotein(a)
- Base Sequence
- CHO Cells
- Cricetinae
- Escherichia coli
- Fibrinogen
- Humans
- Kringles
- Lipoprotein(a)
- Lysine
- Molecular Sequence Data
- Mutation
- Recombinant Proteins