PulseExploreJournal ClubDebatesTrendingResearchersJournals
Instagram
HomeExploreJournal ClubTrending
Synapse
⌘+K
Synapse
March 1, 1984Journal of Biological Chemistry193 citationsOpen Access

Myristylation of the membrane form of a Trypanosoma brucei variant surface glycoprotein.

View Full Paper
MFMichael A. J. FergusonGCGeorge Cross

Key Points

Key points are not available for this paper at this time.

Abstract

A variant surface glycoprotein (VSG) of the parasitic protozoan Trypanosoma brucei was purified following the direct solubilization of trypanosomes in a boiling detergent solution. This material behaved as the amphiphilic membrane form of the glycoprotein previously described (Cardoso de Almeida, M. L., and Turner, M. J. (1983) Nature (Lond.) 302, 349-352). Analysis of this material showed that it contained ester-linked tetradecanoic (myristic) acid. After biosynthetic labeling of trypanosomes with 3Hmyristic acid, it was shown that the release of the VSG coat from the parasite membrane, as the soluble form of the VSG, occurred concomitantly with the loss of myristic acid from the glycoprotein. The results suggest that VSG is attached to the parasite membrane via a covalently linked myristic acid-containing lipid moiety.

Ask AI
Helpful
Bookmark
Share
View Full Paper

Cite This Study

Ferguson et al. (1984) studied this question.

synapsesocial.com/papers/6a7013418031ec7bb1dc186fhttps://doi.org/10.1016/s0021-9258(17)43250-9
Ask AI
Helpful
Bookmark
Share
View Full Paper