Purification of thrombospondin receptor (CD36) from human platelet membrane

Cited 0 time in scopus
Metadata Downloads
Purification of thrombospondin receptor (CD36) from human platelet membrane
Joongho Kim; Kyoungho Suk; Na-Young Park; Seung Ho Kim
Bibliographic Citation
Experimental and Molecular Medicine, vol. 29, no. 1, pp. 31-34
Publication Year
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.
CD36glycoprotein IV (GPIV)plateletsthrombosisthrombospondin receptor
Springer-Nature Pub Group
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.

Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.