Purification of thrombospondin receptor (CD36) from human platelet membrane

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Title
Purification of thrombospondin receptor (CD36) from human platelet membrane
Author(s)
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
1997
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.
Keyword
CD36glycoprotein IV (GPIV)plateletsthrombosisthrombospondin receptor
ISSN
I000-0028
Publisher
Springer-Nature Pub Group
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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