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Isolation and characterization of the alpha and beta chains of human platelet glycoprotein Ib.
Human platelet glycoprotein Ib has been purified in milligram amounts from platelets obtained by pheresis of thrombocytotic donors. Purification steps included lectin (wheat germ agglutinin) and immuno (murine monoclonal anti-glycoprotein Ib antibody)-affinity chromatography. The disulfide-linked individual alpha and beta chains of GPIb were separated and the amino-terminal amino acid sequence of each chain was determined. Rabbit polyclonal antibody directed against each individual chain was prepared by affinity chromatography and shown to be monospecific by western blot analysis using whole platelet lysate as antigen. These studies outline a useful approach to isolate and characterize the individual chains of GPIb.
PMID: 3632685 [PubMed - indexed for MEDLINE]
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Cited by 2 PubMed Central articles
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Platelet glycoprotein ibalpha is a counterreceptor for the leukocyte integrin Mac-1 (CD11b/CD18).
Simon DI, Chen Z, Xu H, Li CQ, Dong J, McIntire LV, Ballantyne CM, Zhang L, Furman MI, Berndt MC, et al.
J Exp Med. 2000 Jul 17; 192(2):193-204.
[J Exp Med. 2000]
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The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence.
Lopez JA, Chung DW, Fujikawa K, Hagen FS, Davie EW, Roth GJ.
Proc Natl Acad Sci U S A. 1988 Apr; 85(7):2135-9.
[Proc Natl Acad Sci U S A. 1988]