Isolation of Two Glycolipid Transfer Proteins from Bovine Brain: Reactivity toward Gangliosides and Neutral Glycosphingolipids

Robert W. Ledeen, Charles M. Gammon, Kuldeep K. Vaswani

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

Two glycolipid transfer proteins that catalyze the transfer of gangliosides and neutral glycosphingolipids from phosphatidylcholine vesicles to erythrocyte ghosts have been isolated from calf brain. Purification procedures included differential centrifugation, precipitation at pH 5.1, ammonium sulfate precipitation, and gel filtration on Sephadex G-50 and G-75. The final stage employed fast protein liquid chromatography (Mono S), producing two peaks of activity. Apparent purity of the major peak (TP I) was approximately 85-90%, as judged by sodium dodecyl sulfate/urea-polyacrylamide gel electrophoresis. That of the minor fraction (TP II) was less. The major band of both fractions had a molecular mass of approximately 20000 daltons. Both proteins catalyzed the transfer of ganglioside GM1 as well as asialo-GMl, but transfer protein I was more effective with di- and trisialogangliosides. Transfer protein II appeared to be somewhat more specific for neutral glycolipids in that GA1 was transferred more rapidly than any of the gangliosides; however, lactosylceramide transfer was relatively slow. Neither protein catalyzed transfer of phosphatidylcholine.

Original languageEnglish (US)
Pages (from-to)6239-6243
Number of pages5
JournalBiochemistry
Volume26
Issue number19
DOIs
StatePublished - 1987
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry

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