Biosynthesis of eukaryotic cell surface glycosphingolipids using solubilized glycosyltransferases.
J Biosci
;
1985 Aug; 8(1&2): 413-424
Article
in English
| IMSEAR
| ID: sea-160406
ABSTRACT
Two fucsyltransferases (FucT-2 and FucT-3) have been solubilized from Golgi-rich membrane fraction of bovine spleen, using a cationic detergent. FucT-3 was distinguished from FucT-2 by comparing their kinetic parameters and heat stability. FucT-2 and FucT-3 lost activity (85 %) and (5 %), respectively, when heated at 55°C for 10 sec. Two galactosyltransferases (GalT-3 and GalT-4) and two sialyltransferases (SAT-2 and SAT-3) have also been solubilized from embryonic chicken brain membranes using nonionic detergents. Affinity chromatography and microisoelectric focusing were used to separate these enzymes into functionally pure fractions. Anomeric and positional linkages in some of the products (LM1 and LD1c) have also been established. The terminal NeuAc(α2–8) linkage in GD3 and LD1c was established by identification of the partially methylated penultimate [Ac-14C]sialic acid.
Full text:
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Index:
IMSEAR (South-East Asia)
Language:
English
Journal:
J Biosci
Year:
1985
Type:
Article
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