Evidence of myristylated disulfide-linked dimer of variant surface glycoprotein of Trypanosoma brucei-brucei

Comp Biochem Physiol B. 1989;92(4):705-10. doi: 10.1016/0305-0491(89)90253-8.

Abstract

1. Variant surface glycoprotein (VSGs) of Trypanosoma brucei-brucei may exist as a disulfide-linked dimer in both forms: myristylated (mfVSG) and non-myristylated (sVSG), as judge by fluorography and immunoblotting of SDS-PAGE under non-reducing conditions. 2. The dimeric VSG form is labeled with [3H]-myristic acid in our incorporation conditions. 3. AnTat 1.1 trypanosomes preincubated with tunicamycin and incubated with [3H]-myristic acid synthesized a labeled molecule that has an apparent molecular weight slightly smaller than the native form, and that also corresponds to a disulfide-linked dimer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • Disulfides / analysis*
  • Electrophoresis, Polyacrylamide Gel
  • Myristates / analysis*
  • Myristic Acids / analysis*
  • Trypanosoma brucei brucei / analysis*
  • Tunicamycin / pharmacology
  • Variant Surface Glycoproteins, Trypanosoma / analysis*

Substances

  • Disulfides
  • Myristates
  • Myristic Acids
  • Variant Surface Glycoproteins, Trypanosoma
  • Tunicamycin