Purification of thrombospondin receptor (CD36) from human platelet membrane.
- Author:
Joong Ho KIM
1
;
Kyoung Ho SUK
;
Na Young PARK
;
Seung Ho KIM
Author Information
1. KIST, KOREA RES INST BIOSCI & BIOTECHNOL, PROT FUNCT RES UNIT/TAEJON 305600, SOUTH KOREA.
- Publication Type:Original Article
- Keywords:
CD36;
glycoprotein IV (GPIV);
platelets;
thrombosis;
thrombospondin receptor
- MeSH:
Adhesives;
Antigens, CD36*;
Blood Coagulation;
Blood Platelets*;
Cell Adhesion;
Cell Line;
Chromatography;
Chromatography, Gel;
Electrophoresis, Polyacrylamide Gel;
Humans*;
Immunodiffusion;
Membrane Proteins;
Membranes*;
Molecular Weight;
Thrombosis;
Thrombospondins*;
Triticum
- From:Experimental & Molecular Medicine
1997;29(1):31-34
- CountryRepublic of Korea
- Language:English
-
Abstract:
Thrombospondin receptor (CD36) has been recently identified in platelets and various cell lines as the receptor for thrombospondin, an adhesive protein required for irreversible aggregation of platelets as well as other adhesive processes. Thrombospondin receptor, one of major glycosylated platelet membrane proteins, is thought to play an important role as a cell adhesion molecule in blood coagulation system as well as intercellular signaling. In this work, thrombospondin receptor was purified to homogeneity from human platelet by wheat germ agglutinin (WGA)-affinity chromatography and size exclusion chromatography on Ultrogel-AcA44. The molecular weight of the purified thrombospondin receptor was about 88 kDa on SDS-PAGE and its identity was confirmed by immunoblot analysis and immunodiffusion assay.
