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https://olympias.lib.uoi.gr/jspui/handle/123456789/8790Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Bakalis, E. | en |
| dc.contributor.author | Kosmas, M. | en |
| dc.contributor.author | Papamichael, E. M. | en |
| dc.date.accessioned | 2015-11-24T16:44:20Z | - |
| dc.date.available | 2015-11-24T16:44:20Z | - |
| dc.identifier.issn | 0092-8240 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/8790 | - |
| dc.rights | Default Licence | - |
| dc.subject | enzyme catalyzed reactions | en |
| dc.subject | transient phase kinetics | en |
| dc.subject | perturbation theory | en |
| dc.subject | variational iteration method | en |
| dc.subject | biochemical reaction model | en |
| dc.subject | steady-state assumption | en |
| dc.subject | cysteine proteinases | en |
| dc.subject | kinetics | en |
| dc.subject | systems | en |
| dc.subject | equations | en |
| dc.title | Perturbation Theory in the Catalytic Rate Constant of the Henri-Michaelis-Menten Enzymatic Reaction | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | DOI 10.1007/s11538-012-9761-x | - |
| heal.identifier.secondary | <Go to ISI>://000310316100001 | - |
| heal.identifier.secondary | http://download.springer.com/static/pdf/92/art%253A10.1007%252Fs11538-012-9761-x.pdf?auth66=1386153529_17ff30b1735786832e784a448673321c&ext=.pdf | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2012 | - |
| heal.abstract | The Henry-Michaelis-Menten (HMM) mechanism of enzymatic reaction is studied by means of perturbation theory in the reaction rate constant k (2) of product formation. We present analytical solutions that provide the concentrations of the enzyme (E), the substrate (S), as well as those of the enzyme-substrate complex (C), and the product (P) as functions of time. For k (2) small compared to k (-1), we properly describe the entire enzymatic activity from the beginning of the reaction up to longer times without imposing extra conditions on the initial concentrations E (o) and S (o) , which can be comparable or much different. | en |
| heal.publisher | Springer Verlag (Germany) | en |
| heal.journalName | Bulletin of Mathematical Biology | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Bakalis-2012-Perturbation Theory.pdf | 788.7 kB | Adobe PDF | View/Open Request a copy |
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