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© Thierry Blisnick & Philippe Bastin, Institut Pasteur
Bloodstream Trypanosoma brucei cell
Publication : Biochemical and biophysical research communications

A rapid method purifies a glycoprotein of Mr 145,000 as the LDL receptor of Trypanosoma brucei brucei

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biochemical and biophysical research communications - 15 Jul 1991

Coppens I, Bastin P, Courtoy PJ, Baudhuin P, Opperdoes FR

Link to Pubmed [PMID] – 2069558

Biochem. Biophys. Res. Commun. 1991 Jul;178(1):185-91

The trypanosome LDL receptor has been isolated from bloodstream form and cultured insect-stage trypanosomes as a protein of Mr 145,000, using a rapid purification procedure in the presence of a cocktail of protease inhibitors, whereas previously a polypeptide of Mr 86,000 was purified as the LDL receptor. Both the 145,000 and the 86,000 polypeptides are glycosylated and recognized by a monospecific antibody raised against the 86,000 species. This antibody inhibits LDL binding to the intact trypanosomes, to the isolated 145,000 receptor and to the 86,000 species. Hence, the previously isolated 86,000 polypeptide is a degradation product probably representing the cleaved-off ectodomain of the trypanosome LDL receptor.

http://www.ncbi.nlm.nih.gov/pubmed/2069558