Tetaert D, Gomes V, Huet-Duvillier G, Demeyer D, Hublart M, Boersma A, Degand P
Biochem Biophys Res Commun. 1987 May 14;144(3):1222-8. doi: 10.1016/0006-291x(87)91441-0.
High performance liquid chromatography (HPLC) procedures have been used to analyze a preparation of the variant surface glycoprotein AnTat 1.1A of Trypanosoma brucei. The native preparation gives several peaks with a high reproducibility both by reverse-phase (RP-) and gel permeation (GP-) HPLC. Under RP-HPLC conditions, nine fractions are fully resolved. The RP-HPLC fractions migrate with the same molecular weight VSG band on polyacrylamide slab gel electrophoresis and no significant differences are observed in amino acid composition among these fractions. The RP-HPLC resolution is found to be related to the ability of the VSG to polymerize as shown using GP-HPLC. These results suggest the existence of a microheterogeneity of the AnTat 1.1A VSG preparation in relation to post-translational modification of the VSG molecule.
