| Origin | recombinant E. coli |
|---|---|
| Lineage name | α-D-Glucoside glucohydrolase |
| EC Number | 3.2.1.20 |
| Reaction formula | α-D-Glucoside + H2O →→→ α-D-Glucose + ROH |
alpha-Glucosidase (aGLS-SE)
- The enzyme is useful for the determination of α-amylase and serum chloride in clinical analysis.
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SPECIFICATION
| Appearance | white lyophilizate | |
|---|---|---|
| Activity | ≧10 U/mg lyophilizate | |
| Contaminant | α-amylase ≦5.0×10-3％ | |
| Stabilizer | albumin from bovine serum | |
| Storage | below -20℃ |
PROPERTIES
| Molecular weight | ca. 61 kDa (gel filtration) |
|---|---|
| Structure | monomer of 60 kDa (SDS-PAGE) |
| Michaelis constant | 5.5×10-5M (p-nitrophenyl-α-D-glucoside) |
| pH Optimum | 6.0–9.0 |
| pH Stability | 5.0–10.0 |
| Optimum temperature | 52–55°C |
| Thermal stability | below 50℃ |
| Stability (liquid form) | stable at 37℃ for at least two weeks |
| Stability (powder form) | stable at 30℃ for at least one month |
| Inhibitors | Hg2+，Ag+ |
| Specificity | 下記表組参照 |
| Specificity | |
|---|---|
| Substrate*a | Relative activity (%)*b |
| PNPG | 100.0 |
| PNPG2 | 9.4 |
| PNPG5 | 1.1 |
| Maltose | 10.2 |
| Maltotriose | 112.9 |
| Maltotetraose | 13.9 |
| Maltopentaose | 1.4 |
a：Substrate concentration, 2.2 mM
b：Glucose-forming activity, pH 7.0 at 37℃
APPLICATIONS
The enzyme is useful for the determination of α-amylase and serum chloride in clinical analysis.
REFERENCES
- Halvorson, H., “Methods in Enzymology,” Vol. 8, Academic Press, New York, 1966, pp. 559–562.
- Ono, T. et al., Clin. Chem., 34, 552–553 (1988).
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