Joziasse D H, Damen H C, de Jong-Brink M, Edzes H T, Van den Eijnden D H
FEBS Lett. 1987 Aug 31;221(1):139-44. doi: 10.1016/0014-5793(87)80368-x.
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 beta-galactose residues. The products formed with lactose (Gal beta 1----4Glc) as the acceptor were characterized by HPLC, and subjected to 400-MHz 1H-NMR and methylation analysis. The main product was shown to have the structure Gal beta 1----3Gal beta 1----4Glc. Therefore, the galactosyltransferase can be identified as a UDP-Gal:beta-galactoside beta 1----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.
椎实螺（Lymnaea stagnalis）蛋白腺的去污剂提取物含有一种酶活性，该活性可将半乳糖从UDP-半乳糖转移至具有末端非还原型β-半乳糖残基的受体底物上。以乳糖（Galβ1→4Glc）作为受体形成的产物通过高效液相色谱（HPLC）进行表征，并进行了400兆赫的1H-核磁共振（1H-NMR）和甲基化分析。结果表明，主要产物的结构为Galβ1→3Galβ1→4Glc。因此，这种半乳糖基转移酶可被鉴定为UDP-半乳糖：β-半乳糖苷β1→3-半乳糖基转移酶。鉴于其连接和受体特异性，该酶可能对乳原的生物合成至关重要，乳原是椎实螺蛋白腺产生的主要多糖。
