The protein-DNA crosslinking capability of cis-dichloro diammineplatinum has been exploited to check the intranuclear location of N-glycosylated proteins. When intact liver cells were treated with this reagent, a number of glycoproteins, recognized by Concanavalin A, have been shown to become crosslinked to DNA; many of them have been recognized as nuclear matrix components. The recognition by this lectin was abolished by treatment with N-glycosidase F, showing the presence of N-glycosidic bonds between the sugar moiety and the protein. Most of the glycoproteins appeared to have high mannose oligosaccharide chains, but sialic acid containing oligosaccharides were also identified.
The presence of N-glycosylated proteins in cell nuclei / Ferraro, Anna; Grandi, P; Eufemi, Margherita; Altieri, Fabio; Cervoni, Laura; Turano, Carlo. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - STAMPA. - 178:(1991), pp. 1365-1370. [10.1016/0006-291X(91)91044-D]
The presence of N-glycosylated proteins in cell nuclei.
FERRARO, Anna;EUFEMI, Margherita;ALTIERI, Fabio;CERVONI, Laura;TURANO, Carlo
1991
Abstract
The protein-DNA crosslinking capability of cis-dichloro diammineplatinum has been exploited to check the intranuclear location of N-glycosylated proteins. When intact liver cells were treated with this reagent, a number of glycoproteins, recognized by Concanavalin A, have been shown to become crosslinked to DNA; many of them have been recognized as nuclear matrix components. The recognition by this lectin was abolished by treatment with N-glycosidase F, showing the presence of N-glycosidic bonds between the sugar moiety and the protein. Most of the glycoproteins appeared to have high mannose oligosaccharide chains, but sialic acid containing oligosaccharides were also identified.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.