Naslov
Interactions of intact human galectin-3 and its C-terminal fragment with oligosaccharides: an electrospray mass spectrometry study

Autori
Jovanović, Marko ; Svensson, Inge ; Leffler, Hakon ; Peter-Katalinić, Jasna

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Abstracts of the GLYCO XVI, XVI international symposium on glycoconjugates / - , 2001

Skup
GLYCO XVI, XVI international symposium on glycoconjugates

Mjesto i datum
Den Haag, Nizozemska, 19.08.2001. - 24.08.2001

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
protein-carbohydrate interactions; Affinity MS; ESI MS

Sažetak
Galectin-3, the beta-galactoside binding protein plays a central role in a variety of biologicla functions including cellular recognition and adhesion, regulation of apoptosis and pre-mRNA splicing. We investigated the structure and properties of two galectin-3 proteins using electrospray ionization mass spectrometry (ESI MS), an established method prociding direct insights in protein structure and its non-covalent complexes. Intact human galectin-3 (G-3) was expressed in E. coli. The C-terminal fragment thereof (G3-C) containing the CRD was produced by collagenase VII digestion. Molecular weight of the intact G-3 was determined by nanoESI-QTOF MS to be 26020.2, indicating the lack of the N-terminal methionine, and the ions assigned to adducts with 1-5 lactose moieties. Similar patterns were obtained with the G-3-C preparation. The stability of the lactose adducts and their non-covalent nature was investigated in an ESI-MS approach by de-/renaturation, by increase of the cone volatage and by collision induced dissociation (CID) experiments. Relative affinities for beta-galactosides were determined under native conditions.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija, Biotehnologija

POVEZANOST RADA