EC Number   |
Application |
Reference |
|---|
   4.2.2.7 | analysis |
detection of heparin and heparinase using a ratiometric fluorescence method based on benzoperylene derivative, 6-(benzo [ghi]perylene-1,2-dicarboxylic imide-yl)hexanoic acid excimer in an aequeous buffer solution. The assay is simple, rapid, inexpensive, sensitive and selective and can be used for assay of heparin and heparinase in complex sample mixtures |
747335 |
| 4.2.2.7 | analysis |
development of a simple and rapid colorimetric method, which can detect heparinase activity and thus help to identify likely candidates for future anti-metastatic and anti-inflammatory drugs |
681722 |
| 4.2.2.7 | analysis |
in heparinized blood plasma samples of cancer patients, heparinase addition removes the heparin inhibition. Treatment significantly improves PCR efficacy, enabling quantification of circulating tumor DNA |
747602 |
| 4.2.2.7 | analysis |
the GSTfused enzyme with high purity and specific activity may be useful in solid phase clinical applications and sequence characterizations of structurally specific heparin and heparan sulfate motifs |
677819 |
| 4.2.2.7 | medicine |
in a murine model of thermal injury, mutation of HepP reduces the rate of mortality from 100% for mice infected with wild-type to 7% for mice infected with the mutant strain. Upon intraperitoneal inoculation of the thermally injured mice, the rate of mortality for mice infected the mutant was 0%, whereas it was 66% for mice infected with wild-type. Only wild-type PA14 is recovered from the livers and spleens of infected mice |
-, 747935 |
| 4.2.2.7 | synthesis |
expression as fusion protein, fused to the C-terminus of soluble partners translation initiation factor 2 domain I, glutathione S-transferase, maltose-binding protein, small ubiquitin modifying protein and N-utilization substance A, and purification of hybrid proteins. Except for NusA, the fusion partners dramatically improve the soluble expression of recombinant HepA, with translation initiation factor 2 domain I-HepA and small ubiquitin modifying protein-HepA creating almost completely soluble HepA where 98% and 94% of expressed HepA fusions are soluble, respectively |
730873 |
| 4.2.2.7 | synthesis |
expression in Escherichia coli using a hexahistidine-tagged small ubiquitin-like modifier. The fusion protein exhibits high enzyme activity without requirements of in vitro refolding and SUMO-tag releasing process, and the optimum enzyme activity is obtained at 30°C, pH 7.0 and 10 mmol/l Ca2+ in the reaction buffer |
747363 |
| 4.2.2.7 | synthesis |
expression of HepI with the chitin binding domain of Bacillus circulans chitinase A1 as a chitin-affinity tag, and the small ubiquitin-like modifier (SUMO) linker as a solvation enhancer in different fusion sequence. The constructs chitin binding domain-HepI, chitin binding domain-SUMO-HepI, SUMO-chitin binding domain-HepI and chitin binding domain-HepI-SUMO show specific enzyme activities of 1.88, 3.69, 3.44, and 2.73 IU/mg total proteins, respectively, with unfractionated heparin as substrate. Chitin binding domain-SUMO-HepI exhibits the maximum half-life (48 min) at 30°C and best thermostability under 15-50°C. All the fusion enzymes show broad pH-stability in the range of 5.4-9.0 |
747940 |
