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Title: Characterization of glycolipid galactosyltransferases from embryonic chicken brain

Thesis/Dissertation ·
OSTI ID:6067863

Glycolipid galactosyltransferases (GalT-3 and GalT-4) were solubilized from a membrane fraction isolated from embryonic chicken brain. The profiles of specific activity and total units per brain of GalT-3 and GalT-4 varied with embryonic age. GalT-4 had the highest specific activity at 9 days of embryonic development and showed a steady decrease until hatching. GalT-3 showed a gradual increase in specific activity. Both GalT3 and GalT-4 showed a steady increase in total units per brain throughout embryonic development. The solubilized enzymes could be separated using gel filtration, ion exchange chromatography or affinity chromatography on ..cap alpha..-lactalbumin-agarose. Data obtained in the study imply that GalT-4 is involved in both glycoprotein and glycolipid biosynthesis. Glycosphingolipid products from GalT-3 and GalT-4 catalyzed reactions labeled with (/sup 14/C)galactose comigrated with authentic GMI and nLcOse/sub 4/Cer, when examined by thin layer chromatography and autoradiography. Studies with galactosidases revealed that all of the enzyme products formed by GalT-3 and GalT-4 contained a (/sup 14/C)-galactose in a ..beta.. anomeric linkage. Periodate oxidation studies of Gal-(/sup 14/C)GlcNAc, formed by purified GalT-4 using (/sup 14/C)GlcNAc as the acceptor, demonstrated that approximately 70% of the linkage formed was Gal..beta..1-4GlcNAc and 30% was Gal..beta..1-3GlcNAc. Studies on the susceptibility of (/sup 14/C)Gal-GlcNAc to base catalyzed ..beta..-elimination also suggested the presence of approximately 30% Gal..beta..1-3GlcNAc.

Research Organization:
Notre Dame Univ., IN (USA)
OSTI ID:
6067863
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English