Evidence of myristylated disulfide-linked dimer of variant surface glycoprotein of Trypanosoma brucei-brucei
| Autor: | Guillemette Huet-Duvillier, Pierre Degand, M. Hublart, Lucia Mendonça-Previato, François Boutignon |
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| Rok vydání: | 1989 |
| Předmět: |
Physiology
Stereochemistry Dimer Blotting Western Trypanosoma brucei brucei Myristic acid Trypanosoma brucei Biochemistry chemistry.chemical_compound parasitic diseases Animals Disulfides Molecular Biology chemistry.chemical_classification Myristates biology Tunicamycin General Medicine biology.organism_classification chemistry Trypanosoma Protozoa Electrophoresis Polyacrylamide Gel PMSF Glycoprotein Myristic Acids Variant Surface Glycoproteins Trypanosoma |
| Zdroj: | Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 92:705-710 |
| ISSN: | 0305-0491 |
| DOI: | 10.1016/0305-0491(89)90253-8 |
| Popis: | 1. 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. 2. The dimeric VSG form is labeled with [ 3 H]-myristic acid in our incorporation conditions. 3. 3. AnTat 1.1 trypanosomes preincubated with tunicamycin and incubated with [ 3 H]-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. |
| Databáze: | OpenAIRE |
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