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Vol. 273, Issue 1, 433-440, January 2, 1998
-Galactosyltransferase Catalyzing the Formation of Type 1 Chains
From Novartis Pharma AG, Transplantation Preclinical Research,
CH 4002 Basel, Switzerland
Biochemical evidence suggests that the
galactosyltransferase activity synthesizing type 1 carbohydrate chains
is separate from the well characterized enzyme that is responsible for
the synthesis of type 2 chains. This was recently confirmed by the cloning, from melanoma cells, of an enzyme capable of synthesizing type
1 chains, which was shown to have no homology to other
galactosyltransferases. We report here the molecular cloning and
functional expression of a second human 
3-galactosyltransferase
distinct from the melanoma enzyme. The new 3-galactosyltransferase
has homology to the melanoma enzyme in the putative catalytic domain,
but has longer cytoplasmic and stem regions and a carboxyl-terminal
extension. Northern blots showed that the new gene is present primarily
in brain and heart. When transfected into mammalian cells, this gene
directs the synthesis of type 1 chains as determined by a monoclonal
antibody specific for sialyl Lewisa. A soluble
version of the cloned enzyme was expressed in insect cells and
purified. The soluble enzyme readily catalyzes the transfer of
galactose to GlcNAc to form Gal(1-3)GlcNAc. It also has a minor but
distinct transfer activity toward Gal, LacNAc, and lactose, but is
inactive toward GalNAc.
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