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. Author manuscript; available in PMC: 2011 Feb 1.
Published in final edited form as: Int J Parasitol. 2009 Aug 18;40(2):215. doi: 10.1016/j.ijpara.2009.07.009

Table 1.

Galactosyltransferase activity in an enzyme extract derived from Haemonchus contortus adult worms

Acceptor Relative galactosyltransferase (GalT) activity
H. contortus GalT Bovine α1,3-GalT
GalNAcα-O-pNP 100a <1
GalNAcβ-O-pNP 13 <1
GalNAcβ1-4GlcNAc-R1b 40 5
Galβ1-4GlcNAc-pNP <1 51
Galβ-O-pNP <1 41
Galα-O-pNP <1 4
Fucα1-2Galβ1-3GlcNAc-R2 <1 1
Fucα1-2Galβ1-4GlcNAc-R1 <1 2
Galβ1-3GlcNAc-R1 <1 100a

All acceptor substrates in the assays have been used at a concentration of 1 mM. The acceptor specificity of the H. contortus enzyme extract has been compared with the activity of commercial bovine (α1,3-galactosyltransferase (α1,3-GalT). For both enzymes, the acceptor substrate that showed the highest activity has been set at 100%. In the assays with H. contortus extract, 100% activity represents an enzyme activity of 1 nmol/ml/h, and for the α1,3-GalT 100% activity represents an activity 49 nmol/ml/h.

a

Values set at 100%

b

R1 = -O-(CH2)8COOCH3; R2 = -(CH2)7CH3