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Acetylcholine Esterase — Dynamic Behaviour with Flow Calorimetry
Malík, F. and Štefuca, V. Acetylcholine Esterase — Dynamic Behaviour with Flow Calorimetry Chemical Papers, Vol.56, No. 6, 2002, 406-411
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Document type:
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Článok z časopisu / Journal Article |
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Collection:
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Chemical papers
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| Attached Files |
| Name |
Description |
MIMEType |
Size |
Downloads |
n566a406.pdf
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566a406.pdf |
application/pdf |
198.02KB |
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| Author(s) |
Malík, F.
Štefuca, V.
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| Title |
Acetylcholine Esterase — Dynamic Behaviour with Flow Calorimetry
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| Journal name |
Chemical Papers
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| Publication date |
2002
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| Year available |
2002
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| Volume number |
56
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| Issue number |
6
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| ISSN |
0366-6352
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| Start page |
406
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| End page |
411
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| Place of publication |
Poland
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| Publisher |
Versita
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| Collection year |
2002
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| Language |
english
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| Subject |
270000 Biological Sciences
270800 Biotechnology
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| Abstract/Summary |
The application of enzyme flow calorimetry for the monitoring of hysteresis behaviour of immobilized enzyme was investigated. The hysteresis of immobilized acetylcholine esterase induced by combination of mass transfer and substrate inhibition was considered. Theoretical analysis of the hysteresis was based on mathematical modelling using kinetic and di usion parameters from literature. The influence of Thiele modulus and the ratio of substrate inhibition and Michaelis constant (Ki/Km) on the size and region of hysteresis was determined. It was shown that by increasing the value of Thiele modulus or Ki/Km, the region of hysteresis was shifted towards higher substrate concentrations. On the basis of the simulation results it was concluded that a commercial preparation of acetylcholine esterase should give rise to hysteresis at value of Thiele modulus higher than 150. The considered particle diameter should be in the range from 0.1 to 1.0 mm.
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