Article
Threonine-145/methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbalpha express HPA-2 epitopes and show equal binding of von Willebrand factor.
Blood - 1 Jan 2000
Li C Q, Garner S F, Davies J, Smethurst P A, Wardell M R, Ouwehand W H
Abstract excerpt
Glycoprotein (GP) Ibalpha is the functionally dominant subunit of the platelet GPIb-IX-V receptor complex, with the von Willebrand factor (vWF) binding site residing on the amino-terminus. A threonine for methionine-145 replacement of GPIbalpha is associated with the human platelet antigen (HPA)-2 system. To study the structural and functional consequences of this mutation, both forms of GPIbalpha were expressed...
Topics
- Amino Acid Substitution
- Animals
- Antibodies
- Antigens, Human Platelet
- Baculoviridae
- Blotting, Western
- Cell Line
- Genetic Variation
- Humans
- Insecta
- Kinetics
- Methionine
- Platelet Glycoprotein GPIb-IX Complex
- Recombinant Proteins