ISSN:
1573-4986
Keywords:
α1–2 fucosyltransferase
;
α1–3 fucosyltransferase
;
haemocyanin
;
Lymnaea stagnalis
;
glycoprotein
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract Connective tissue of the freshwater pulmonateLymnaea stagnalis was shown to contain fucosyltransferase activity capable of transferring fucose from GDP-Fuc in α1–2 linkage to terminal Gal of type 3 (Galβ1–3GalNAc) acceptors, and in α1–3 linkage to GlcNAc of type 2 (Galβ1–4GlcNAc) acceptors. The α1–2 fucosyltransferase was active with Galβ1–3GalNAcβ1-OCH2CH=CH2 (K m=12 mM,V max=1.3 mU ml−1) and Galβ1–3GalNAc (K m=20 mM,V max=2.1 mU ml−1), whereas the α1–3 fucosyltransferase was active with Galβ1–4GlcNAc (K m=23 mM,V max=1.1 mU ml−1). The products formed from Galβ1–3GalNAcβ1-OCH2CH=CH2 and Galβ1–4GlcNAc were purified by high performance liquid chromatography, and identified by 500 MHz1H-NMR spectroscopy and methylation analysis to be Fucα1–2Galβ1–3GalNAcβ1-OCH2CH=CH2 and Galβ1–4(Fucα1–3)GlcNAc, respectively. Competition experiments suggest that the two fucosyltransferase activities are due to two distinct enzymes.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01049686
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