Molecular heterogeneity of the isolated surface glycoprotein from variant AnTat 1.1 of Trypanosoma brucei brucei

1 January 1988

journal article
Published by Wiley in Biology of the Cell

Vol. 64 (2) , 131-135
https://doi.org/10.1016/0248-4900(88)90072-x

Abstract

Variant surface glycoprotein (VSG) of Trypanosoma brucei brucei AnTat 1.1 was released by means of the procedure described by Baltz et al. ([1976], Ann. Immunol. [Inst. Pasteur] 127C, 761–774). The concanavalin-A chromatography yielded 3 VSG fractions according to the addition, in the elution buffer, of α-methyl-d-mannopyranoside, β-mercaptoethanol, and sodium dodecyl sulfate. These VSG fractions showed heterogeneous behaviour on reverse-phase high performance liquid chromatography. The 3 VSG fractions as well as the myristylated VSG of AnTat 1.1 essentially consist of dimer VSG forms linked through a disulfide bridge, as judged by sodium dodecyl sulfate polyacrylamide gel electrophoresis, under reducing and nonreducing conditions.

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