Glycosylation and deglycosylation of proteasomes (prosomes) from calf-liver cells: high abundance of neuraminic acid.

Hp Schmid , R Vallon , W Tomek , C Kreutzer-Schmid , Mn Pouch , S. S. Badaoui (1) , G. Boissonnet (2) , M Briand , Y Briand , J Buri

1 GDEC - Génétique Diversité et Ecophysiologie des Céréales
2 CEA-DES (ex-DEN) - CEA-Direction des Energies (ex-Direction de l'Energie Nucléaire)

Proteasomes (prosomes) of calf-liver cells were probed with three different biotinylated lectins: Limulus polyphemus agglutinin (LPA), specific for neuraminic acid; Solanum tuberosum agglutinin (STA), specific for GlcNac; and concanavalin A (Con A), specific for Man/Glc. While only one proteasomal protein reacted with STA, most of the proteasomal proteins reacted with LPA and several with Con A. Deglycosylation with N-glycosidase F showed that the detected glycan residues were asparagine-linked. Finally we demonstrate an alternative method for the isolation of proteasomes based on the affinity of certain proteasomal proteins to Con A.

Domaines: Sciences du Vivant [q-bio]; Biochimie, Biologie Moléculaire

Hp Schmid, R Vallon, W Tomek, C Kreutzer-Schmid, Mn Pouch, et al.. Glycosylation and deglycosylation of proteasomes (prosomes) from calf-liver cells: high abundance of neuraminic acid.. Biochimie, 1993, pp.905-10. ⟨hal-01919721⟩