Glycosylation and deglycosylation of proteasomes (prosomes) from calf-liver cells: High abundance of neuraminic acid
1993; Elsevier BV; Volume: 75; Issue: 10 Linguagem: Inglês
10.1016/0300-9084(93)90047-v
ISSN1638-6183
AutoresHans Peter Schmid, Rüdiger Vallon, Wolfgang Tomek, Claudia Kreutzer-Schmid, Mn Pouch, Saloua Badaoui, Gérard Boissonnet, M. Briand, Yves Briand, Jacques Buri,
Tópico(s)Ubiquitin and proteasome pathways
ResumoProteasomes (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.
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