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A rapid method purifies a glycoprotein of Mr145,000 as the LDL receptor ofTrypanosoma brucei brucei

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
178
Issue
1
Identifiers
DOI: 10.1016/0006-291x(91)91797-g
Disciplines
  • Biology

Abstract

Abstract The trypanosome LDL receptor has been isolated from bloodstream form and cultured insect-stage trypanosomes as a protein of M r 145,000, using a rapid purification procedure in the presence of a cocktail of protease inhibitors, whereas previously a polypeptide of M r 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.

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