Isolation of a type IV collagen binding protein from human platelets.
Indian J Biochem Biophys
;
1991 Oct-Dec; 28(5-6): 531-5
Artículo
en Inglés
| IMSEAR
| ID: sea-27686
ABSTRACT
In order to study the molecular basis of platelet interaction with collagen IV of the basement membrane separating the arterial endothelium from the underlying subendothelial connective tissue, the possibility of presence of platelet membrane protein with affinity to type IV collagen was examined by subjecting the platelet membrane extract to affinity chromatography on collagen IV-sepharose. Urea (4 M) eluate was found to contain a protein with an apparent mol. wt of 68 kDa. The radioiodinated protein was isolated and used to test its specificity. By dot blot assay on nitrocellulose disks and solid-phase assays, the 68 kDa protein was found to bind with high affinity to collagen IV. Lack of significant binding to fibronectin and laminin when compared to albumin control indicated its high specificity for collagen. The radioiodinated protein was inserted into egg yolk lecithin liposomes. While these liposomes attached to microtitre plates coated with collagen IV, there was no significant binding to fibronectin or laminin coated wells, suggesting the membrane associated character of the protein as well as its specificity for collagen. These results indicate that presence of a 68 kDa protein in platelet membrane which interacts with very high specificity to collagen IV.
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Asunto principal:
Plaquetas
/
Humanos
/
Colágeno
/
Receptores de Superficie Celular
/
Receptores de Colágeno
/
Peso Molecular
Idioma:
Inglés
Revista:
Indian J Biochem Biophys
Año:
1991
Tipo del documento:
Artículo
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