Stability and reconstitution of the soluble variant surface glycoprotein (sVSG) from Trypanosoma brucei.

@article{Rehaber1990StabilityAR,
  title={Stability and reconstitution of the soluble variant surface glycoprotein (sVSG) from Trypanosoma brucei.},
  author={P Rehaber and N Staudacher and Robert Seckler and Roger Buelow and Peter Overath and R. C. A. Jaenicke},
  journal={Biochemistry},
  year={1990},
  volume={29 36},
  pages={8217-23}
}
Soluble variant surface glycoprotein (sVSG) is the form of the coat protein of Trypanosoma brucei released by cleavage of its lipid anchor. As shown by ultracentrifugal analysis, the protein of the variant clone MITat 1.2 is a stable dimer of (117 +/- 6)-kDa molecular mass. Its quaternary structure remains unaltered in the concentration range from 0.01 to approximately 50 mg/mL. Further extrapolation to the in situ concentration on the cell surface points to no significant protein association… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.

Similar Papers

Loading similar papers…