Placement Instability Among Young People Removed from Their Original Family and the Likely Mental Health Implications.

Background: Young people in out-of-home care are more likely to experience poorer mental and physical health outcomes related to their peers. Stable care environments are essential for ameliorating impacts of disruptive early childhood experiences, including exposure to psychological trauma, abuse and neglect. At present there are very few high quality data regarding the placement stability history of young people in out-of-home care in Australia or other countries.

Enzymatic glycosylation, inhibitor design, and synthesis and formation of glyco-self assembled monolayers for simulation of recognition.

Glycosyltransferases from the albumen gland of Helix pomatia could be used in tandem mode for the chemoenzymatic synthesis of beta,1-3/beta,1-6-linked oligogalactans. By employing recombinant trans-sialidase of Trypanosoma cruzi (TcTS) the formation of a range of modified Galbeta,1-3GalNAc derivatives could be terminally alpha,2-3 sialylated. Biacore studies indicated the binding of these modified trisaccharides to myelin-associated glycoprotein (MAG).

Tandem exploitation of Helix pomatia glycosyltransferases: facile syntheses of H-antigen-bearing oligosaccharides.

Snails from the family Helicidae produce in their albumen glands a highly branched galactan, which consists almost exclusively of D- and L-galactose. The D-Gal residues are glycosydically beta(1-->6)- or beta(1-->3)-linked, whereas the L-Gal moieties are attached alpha(1-->2). Up until the present time, two beta(1-->6)-D-galactosyl transferases and one alpha(1-->2)-L-galactosyl transferase have been identified in a membrane preparation of these glands.

Fast and efficient synthesis of a novel homologous series of L-fucosylated trisaccharides using the Helix pomatia alpha-(1-->2)-L-galactosyltransferase.

The alpha-(1-->2)-L-galactosyltransferase from the albumen gland of the vineyard snail Helix pomatia exhibits high alpha-(1-->2)-L-fucosyltransferase activity and can be used to transfer L-fucose from GDP-L-fucose to terminal, non-reducing D-galactose residues of an oligosaccharide, thus providing facile access to a range of H-antigen-containing oligosaccharides. The enzymatic glycosylation was applied here on a milligram scale to a series of disaccharide acceptor substrates. Apparently the site of interglycosidic linkage between the terminal and subterminal acceptor sugar units is of little or no consequence.