Trypanosoma brucei brucei: Variability in the association of some variant surface glycoproteins

Autor: Guillemette Huet-Duvillier, Pascal Mathon, Daniel Tetaert, Arnold Boersma, Véronique Gomes, Pierre Degand
Rok vydání: 1988
Předmět:
Zdroj: Experimental Parasitology. 67:31-38
ISSN: 0014-4894
DOI: 10.1016/0014-4894(88)90005-7
Popis: In our isolation procedure, the surface antigens of the variants AnTat 1.1 and 1.10 ( Trypanosoma brucei brucei ) are essentially obtained as a disulfide-linked dimer while the AnTat 1.8 surface antigen is found as a mixture of monomer and disulfide-linked dimer. This observation may be related to the localization of the cysteine residues in the protein sequences. In the purification procedure using concanavalin-A Sepharose chromatography, besides the VSG elution by methyl-α- d -mannopyranoside, a quantitative elution of still bound VSG may be obtained by the addition of β-mercaptoethanol to methyl-α- d -mannopyrannoside in the elution buffer. The surface antigen of the variant AnTat 1.1 was examined for molecular form at several different times during the release procedure. The disulfide-linked dimer could be observed within 30 min of the surface coat release, indicating its presence within the parasite.
Databáze: OpenAIRE