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

Isabelle Coppens, Ph Bastin, P. J. Courtoy, P. Baudhuin, F. R. Opperdoes

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)185-191
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume178
Issue number1
DOIs
StatePublished - Jul 15 1991
Externally publishedYes

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Trypanosoma brucei brucei
Trypanosomiasis
LDL Receptors
Glycoproteins
Peptides
Antibodies
Protease Inhibitors
Purification
Insects
Degradation
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A rapid method purifies a glycoprotein of Mr 145,000 as the LDL receptor of Trypanosoma brucei brucei. / Coppens, Isabelle; Bastin, Ph; Courtoy, P. J.; Baudhuin, P.; Opperdoes, F. R.

In: Biochemical and Biophysical Research Communications, Vol. 178, No. 1, 15.07.1991, p. 185-191.

Research output: Contribution to journalArticle

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