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The β1,6‐GlcNAc transferase activity present in hog gastric mucosal microsomes catalyses site‐specific branch formation on a long polylactosamine backbone
Author(s) -
Helin J,
Penttilä L,
Leppänen A,
Maaheimo H,
Lauri S,
Costello C.E,
Renkonen O
Publication year - 1997
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/s0014-5793(97)00818-1
Subject(s) - chemistry , transferase , microsome , biochemistry , stereochemistry , affinities , enzyme
We find that the β1,6‐GlcNAc transferase activity present in hog gastric mucosal microsomes converts the linear pentasaccharide GlcNAcβ1‐3Galβ1‐4GlcNAcβ1‐3Galβ1‐4GlcNAc (1) in a site‐specific way to the branch‐bearing hexasaccharide GlcNAcβ1‐3(GlcNAcβ1‐6)Galβ1‐4GlcNAcβ1‐3Galβ1‐4GlcNAc (2). The product is a positional isomer of GlcNAcβ1‐3Galβ1‐4GlcNAcβ1‐3(GlcNAcβ1‐6)Galβ1‐4GlcNAc (3), reportedly formed from 1 by another polylactosamine β1,6‐GlcNAc transferase activity present in human serum (Leppänen et al., Biochemistry , 30 (1991) 9287). Combined use of the two kinds of activities gave in the present experiments the heptasaccharide GlcNAcβ1‐3(GlcNAcβ1‐6)Galβ1‐4GlcNAcβ1‐3(GlcNAcβ1‐6)Galβ1‐4GlcNAc (4), in which one of the branches occupies the position of the branch in 2 and the other the position of the branch in 3.