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.