ISSN:
1573-4986
Schlagwort(e):
sialyltransferase
;
glycorprotein
;
baculovirus
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Chemie und Pharmazie
Notizen:
Abstract Values ofK m were determined for three purified sialyltransferases and the corresponding recombinant enzymes. The enzymes were Galβ1-4GlcNAc α2-6sialyltransferase and Galβ1-3(4)GlcNAc α2-3sialyltransferase from rat liver; these enzymes are responsible for the attachment of sialic acid to N-linked oligosaccharide chains; and the Galβ1-3GalNAc α2-3sialyltransferase from porcine submaxillary gland that is responsible for the attachment of sialic acid to O-linked glycoproteins and glycolipids. A procedure for the large scale expression of active sialyltransferases from recombinant baculovirus-infected insect cells is described. For the liver enzymes values ofK m were determined using rat and human asialoα1 acid glycoprotein andN-acetyllactosamine as variable substrates; lacto-N-tetraose was also used with the Galβ1-3(4)GlcNAc α2-3sialyltransferase. Antifreeze glycorprotein was used as the macromolecular acceptor for the porcine enzyme. Values forK m were also determined using CMP-NeuAc as the variable substrate.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00731235
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