Open AccessRapid processing of the carboxyl terminus of a trypanosome variant surface glycoprotein.
Author(s) -
James D. Bangs,
Dale Hereld,
Jessica L. Krakow,
Gerald W. Hart,
Paul T. Englund
Publication year - 1985
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.82.10.3207
Subject(s) - glycoprotein , biochemistry , glycolipid , chemistry , polyacrylamide gel electrophoresis , covalent bond , n terminus , myristic acid , methionine , gel electrophoresis , translation (biology) , peptide sequence , biology , microbiology and biotechnology , amino acid , enzyme , fatty acid , organic chemistry , palmitic acid , messenger rna , gene
The variant surface glycoprotein of the parasite Trypanosoma brucei contains a glycolipid of unknown structure covalently attached to its COOH terminus. We have shown, by using metabolic labeling with [35S]methionine or [3H]myristic acid, precipitation with specific antibodies, and NaDodSO4/polyacrylamide gel electrophoresis, that this glycolipid is attached to the variant surface glycoprotein polypeptide within 1 min after its translation.