Pregled bibliografske jedinice broj: 48410
Comparison of mammalian serum esterases hydrolyzing acylated monosaccharides
Comparison of mammalian serum esterases hydrolyzing acylated monosaccharides // 20th Anniversary Meeting of Croatian Biochemical Society
Zagreb, Hrvatska, 1996. str. - (poster, domaća recenzija, sažetak, znanstveni)
CROSBI ID: 48410 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Comparison of mammalian serum esterases hydrolyzing acylated monosaccharides
Autori
Krstanović, Marina ; Tomašić, Jelka ; Tomić, Srđanka
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
20th Anniversary Meeting of Croatian Biochemical Society
/ - , 1996
Skup
20th Anniversary Meeting of Croatian Biochemical Society
Mjesto i datum
Zagreb, Hrvatska, 18.10.1996. - 19.10.1996
Vrsta sudjelovanja
Poster
Vrsta recenzije
Domaća recenzija
Ključne riječi
mammalian serum ; esterases ; monosaccharides
Sažetak
Esterases of different specifity and activity are present in mammalian sera. In our previous studies we have described and characterized the esterases which could be used for deacylation of pivaloylated and acylated monosaccharides. The aim of the present study was to compare the activities of esterases originating from different mammals, as well as human serum. The deacylation was monitored throughout the experiments using methyl 2, 6-di-O- pivaloyl-a-D-(U-14C)glucopyranoside (2, 6-DP)as the representative substrate. Rabbit and guinea pig sera exhibited high esterase activities (characterized as carboxyl esterases). More detailed chromatgraphic analysis revealed the marked difference between these two sources ; rabbit serum contained one major peak which preferentially hydrolysed 6-O-pivaloyl group in 2, 6-DP, while in guinea pig serum two prominent peaks of activity were detected and one preferentially hydrolysed 2-O-pivaloyl group. Even more striking difference was noticed when human and sheep sera were examined, since the major event observed was the migration of 2-O-pivaloyl group to the position 4- in the sugar molecule, followed by very slow deesterification.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
POVEZANOST RADA
Projekti:
021002
Ustanove:
Imunološki zavod d.d.,
Prirodoslovno-matematički fakultet, Zagreb