BMB Reports
- 제31권5호
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- Pages.515-518
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- 1998
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- 1976-670X(eISSN)
Analysis of the Potent Platelet Glycoprotein IIb-IIIa Antagonist from Natural Sources
- Kang, In-Cheol (Department of Biochemistry, College of Science, and Bioproducts Research Center, Yonsei University) ;
- Kim, Doo-Sik (Department of Biochemistry, College of Science, and Bioproducts Research Center, Yonsei University)
- 투고 : 1998.05.18
- 심사 : 1998.06.05
- 발행 : 1998.09.30
초록
Adhesive interaction of the platelet glycoprotien IIb-IIIa (GP IIb-IIIa) with a plasma protein, such as fibrinogen, plays an important role in thrombosis and hemostasis. The specific sequence Arg-Gly-Asp (RGD) is critical for the binding of fibrinogen to platelet. To examine and characterize the GP IIb-IIIa antagonist from natural sources, we have developed a simple enzyme-linked immunosorbant assay (ELISA) system. The GP IIb-IIIa complex was purified to homogeneity from platelet Iysates by the combination of two affinity chromatographic methods using the synthetic RGD peptide (GRGDSPK)-immobilized Sepharose and wheat germ lectin-Sepharose. The synthetic peptide GRGDSP inhibits GP IIb-IIIa binding to immobilized fibrinogen with an