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Identification of a UDP‐Gal:β‐Galactoside βl→3‐galactosyltransferase in the albumen gland of the snail Lymnaea stagnalis
Author(s) -
Joziasse David H.,
Damen Hanny C.M.,
de Jong-Brink Marijke,
Edzes Hommo T.,
Van den Eijnden Dirk H.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80368-x
Subject(s) - lymnaea stagnalis , snail , biology , lymnaea , galactosyltransferase , identification (biology) , galactoside , zoology , anatomy , ecology , biochemistry , enzyme
Detergent extracts of the albumen gland of the snail Lymnaea stagnalis contain an enzyme activity that transfers Gal from UDP‐Gal to acceptor substrates with terminal non‐reducing β‐galactose residues. The products formed with lactose (Galβl→4Glc) as the acceptor were characterized by HPLC, and subjected to 400‐MHz 1 H‐NMR and methylation analysis. The main product was shown to have the structure Gal‐βl→3Galβl→4Glc. Therefore, the galactosyltransferase can be identified as a UDP‐Gal:β‐galactoside βl→3‐galactosyltransferase. In view of its linkage and acceptor specificity, the enzyme may be essential to the biosynthesis of galactogen, the main polysaccharide produced by albumen glands of L. stagnalis .