Purification of thrombospondin receptor (CD36) from human platelet membrane

Joongho Kim; Kyoungho Suk; Na Young Park; Seung Ho Kim

doi:10.1038/emm.1997.5

Purification of thrombospondin receptor (CD36) from human platelet membrane

Joongho Kim, Kyoungho Suk, Na Young Park, Seung Ho Kim

Department of Medicine

Korea Institute of Science and Technology

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

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.

Original language	English
Pages (from-to)	31-34
Number of pages	4
Journal	Experimental and Molecular Medicine
Volume	29
Issue number	1
DOIs	https://doi.org/10.1038/emm.1997.5
State	Published - 1997

Keywords

CD36
G]ycoprotein IV (GPIV)
Platelets
Thrombosis
Thrombospondin receptor

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10.1038/emm.1997.5

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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.",

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AU - Kim, Joongho

AU - Suk, Kyoungho

AU - Park, Na Young

AU - Kim, Seung Ho

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AB - 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.

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Purification of thrombospondin receptor (CD36) from human platelet membrane

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