Pregled bibliografske jedinice broj: 17127
Digoxin derivatives as a tool to study carbohydrate-lectin interactions
Digoxin derivatives as a tool to study carbohydrate-lectin interactions // Knjiga sažetaka HB98 / . (ur.).
Osijek: Hrvatsko biokemijsko društvo, 1998. (pozvano predavanje, domaća recenzija, sažetak, znanstveni)
CROSBI ID: 17127 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Digoxin derivatives as a tool to study carbohydrate-lectin interactions
Autori
Lauc, Gordan
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Knjiga sažetaka HB98
/ . - Osijek : Hrvatsko biokemijsko društvo, 1998
Skup
HB98 Godišnji sastanak Hrvatskog biokemijskog društva
Mjesto i datum
Bizovac, Hrvatska, 17.09.1998. - 20.09.1998
Vrsta sudjelovanja
Pozvano predavanje
Vrsta recenzije
Domaća recenzija
Ključne riječi
digoxin; glycoprobes; lectins; glycobiology
Sažetak
Glycoconjugates are important in many vital physiological processes of multicellular organisms, from fertilization and development, to modulation of immune functions and memory consolidation. Structures of complex carbohydrates attached to glycoconjugates display specific changes in many diseases, and the investigation of their functions under pathological condition is expected to provide many important data for better understanding of the underlying mechanisms.
One of the proposed functions of the carbohydrate structures on glycoconjugates is the transfer of information through interaction with specific lectin receptors. However, the number of elucidated functional lectin-carbohydrate interactions is still relatively small, and it appears that one of the main problems is the lack of adequate methods to identify lectin activity in complex biological samples.
Digoxin and its deglycosylated derivative digoxigenin are widely used as immunochemical markers for detection of proteins and nucleic acids. To combine the ease of digoxin detection with the specificity of interaction between complex oligosaccharides and lectins we have prepared a series of photoaffinity glycoprobes containing different oligosaccharide structures. When incubated in dark, oligosaccharide part of the glycoprobe forms a complex with lectin receptors. After illumination, covalent link between the probe and the lectin is formed, resulting in a lectin with covalently incorporated digoxin tag. Using antibodies against digoxin this complex can easily be identified immunocytochemically, on Western blots, or affinity purified, making the glycoprobe an useful tool for the study of lectins.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
POVEZANOST RADA