Abstract
A β-(1 → 6)- d - galactosyltransferase has been purified over 2000-fold by affinity chromatography on UDP- p-aminophenyl-Sepharose. The enzyme, from a pellet fraction (8000 × g) of Helix pomatia albumen gland, catalyzes transfer of d-galactose from UDP-galactose to a (1 → 6) linkage on acceptor H. pomatia galactogen. Three other polymers served as acceptors: beef lung galactan, Lymnaea stagnalis galactogen and arabinogalactan from larch wood. To determine the linkage specificity of the enzyme, it was incubated with UDP- d-galactose and acceptor galactogen that had been tritiated previously by treatment with galactose oxidase and [ 3H]KBH 4. The [ 3H]galactogen reaction product was recovered, methylated, hydrolyzed and acetylated; tritiated derivatives were identified by mass spectroscopy of effluent fractions separated by gas chromatography. This analysis revealed that (1 → 6)-linked galactosyl groups had been added to the enzyme-treated acceptor galactogen. Also identified was a hydrolytic enzyme that removed terminal α1,2-linked l-galactosyl residues from H. pomatia galactogen.
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