Comparative study of the N-glycoprotein synthesis through dolichol intermediates in mitochondria, Golgi apparatus-rich fraction and endoplasmic reticulum-rich fraction.
1. Glycosylation of endogenous dolichol acceptors was higher in mitochondria than in C 30,000 g (Golgi apparatus-rich fraction) and C 100,000 g (endoplasmic reticulum-rich fraction). 2. In mitochondria, N-glycoprotein biosynthesized were composed of high mannose type and non-fucosylated biantennary complex type while in C 30,000 g and C 100,000 g preparations, they contained biantennary complex type as tri and tetraantennary complex type oligosaccharides in both fucosylated and non-fucosylated forms.
Levrat
C
C
Department of Biochemistry, University of Lyon, INSERM-CNRS U. 189, Lyon-Sud Medical School, Oullins, France.
Ardail
D
D
Louisot
P
P
D000818:Animals; D001216:Asparagine / Q000032:analysis; D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004286:Dolichols / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005260:Female; D005643:Fucose / Q000032:analysis; D006020:Glycopeptides / Q000302:isolation & purification; D006023:Glycoproteins / Q000096:biosynthesis*; D006056:Golgi Apparatus / Q000378:metabolism*; D006596:Hexosaminidases; D006868:Hydrolysis; D066298:In Vitro Techniques; D008358:Mannose / Q000032:analysis; D051379:Mice; D008815:Mice, Inbred Strains; D008930:Mitochondria, Liver / Q000378:metabolism*; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000302:isolation & purification; D013347:Subcellular Fractions / Q000378:metabolism
D004286:Dolichols; D006020:Glycopeptides; D006023:Glycoproteins; D009844:Oligosaccharides; D005643:Fucose; D001216:Asparagine; D006596:Hexosaminidases; D008358:Mannose