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β1-3,4 Galactosidase, cloned from bovine testis and also known as BTG, is a highly specific exoglycosidase that catalyzes the hydrolysis of terminal β1-3 and β1-4 linked galactose residues from oligosaccharides.
Cloned from bovine testis and expressed in Pichia pastoris (1).
The following reagents are supplied with this product:
| Store at (°C) | Concentration | |
| GlycoBuffer 4 | -20 | 10X |
One unit is defined as the amount of enzyme required to cleave > 95% of the terminal, β-D-galactose from 1 nmol Galβ1-4GlcNAcβ1-3Galβ1-4Glc-7-amino-4-methyl-coumarin (AMC), in 1 hour at 37°C in a total reaction volume of 10 µl.
1X GlycoBuffer 4
1X GlycoBuffer 4:
0.5 M sodium acetate
pH 4.5 @ 25°C
4°C
20 mM Tris-HCl
50 mM NaCl
1 mM EDTA
pH 7.5 @ 25°C
65°C for 10 min
Theoretical: 71 kDa
Two fold dilutions of β1-3,4 Galactosidase are incubated with 1 nmol AMC-labeled substrate and 1X GlycoBuffer 4 in a 10 µl reaction. The reaction mix is incubated at 37°C for 1 hour. Separation of reaction products are visualized via thin layer chromatography (2).
1. The optimal pH for β1-3,4 Galactosidase is 4.5.
2. Although rare in nature, β1-6 linked galactose residues have been shown to be hydrolyzed by β1-3,4 Galactosidase at a much slower rate than β1-3 or β1-4 linked galactose residues (3).
3. Reactions may be scaled-up linearly to accommodate larger reaction volumes.
4. The amount of exoglycosidase enzyme required varies when different substrates are used. Start with 1-2 μl for 1 µg of glycoprotein or 100 nM of oligosaccharide for one hour in a 10-25 μl reaction. If there is still undigested material, let the reaction go overnight.
5. β1-3,4 Galactosidase is a glycosylated protein.
1. Vainauskas, S. New England Biolabs, Inc. Unpublished observation
2. Wong-Madden, S.T. and Landry, D. (1995). Glycobiology. 5, 19-28.
3. Distler, J. and Jourdian, G. (1973). J. Biol. Chem. 248, 6772-6780.
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