The β1,6‐GlcNAc transferase activity present in hog gastric mucosal microsomes catalyses site‐specific branch formation on a long polylactosamine backbone

FEBS Letters

Penttilä, L²  Costello, C.E¹  Leppänen, A²  Maaheimo, H²  Renkonen, O²  Lauri, S²  Helin, J² 

[1] Mass Spectrometry Resource, Boston University School of Medicine, Boston, MA 02118-2394, USA;Institute of Biotechnology, P.O. Box 56, University of Helsinki, Helsinki FIN-00014, Finland

关键词: Polylactosamine;    Backbone branching;    β1;    6-GlcNAc transferase;    Site-specificity;    G and Gal;    d-galactose;    GlcNAc and GN;    N-acetyl-d-glucosamine;    Lac;    lactose;    LacNAc;    Galβ1-4GlcNAc;    NMR;    nuclear magnetic resonance;    MALDI;    matrix-assisted laser desorption/ionization;    ManNAc;    N-acetyl-d-mannosamine;    MH;    maltoheptaose;    MP;    maltopentaose;    MT;    maltotriose;    MTet;    maltotetraose;    MS;    mass spectrometry;    TOF;    time-of-flight;   

DOI  :  10.1016/S0014-5793(97)00818-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown