All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Kinetics of Hydrolysis of Acetylthiocholine and Acetylcholine by Cholinesterases.

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F05%3A00002848" target="_blank" >RIV/00216275:25310/05:00002848 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Kinetics of Hydrolysis of Acetylthiocholine and Acetylcholine by Cholinesterases.

  • Original language description

    Kinetics of hydrolysis of acetylthiocholine (ATCH) and acetylcholine (ACH) by butyrylcholinesterase (BCHE) and acetylcholinesterase (ACHE) are studied. ATCH is used for testing of enzymatic hydrolysis of ACH in vitro, because mechanism of ATCH hydrolysisis qualitatively similar to ACH and its reaction course can be quantitatively on-line measured by two independent methods: spectrophotometrical (determination of thiocholine - product of ATCH hydrolysis - using Ellman´s method) and electrochemical (determination of acetic acid - product of ATCH hydrolysis - by pH-stat method). All tested hydrolyses correspond to the Michaelis-Menten´s equation with the second irreversible step up to the total exhaustion of the substrate. The correlations were made by means of differential and integral kinetic equations describing Michaelis-Menten model. The optimal values of Michaelis constant (KM), maximum velocity (Vm), kinetic constants of single reaction steps and absolute concentration of the used

  • Czech name

    Kinetika hydrolýzy acetylthiocholinu a acetylcholinu pomocí cholinesteráz

  • Czech description

    Byla sledována kinetika enzymatické hydrolýzy acetylthiocholinu a acetylcholinu cholinesterázami. Všechny testované hydrolýzy splňují až do totálního vyčerpání substrátu model Michaelis-Mentenové s druhým irreversibilním krokem. Na základě experimentálních dat byly vypočteny optimální hodnoty Michaelisovy konstanty KM, maximální rychlost Vm a kinetické konstanty jednotlivých reakčních kroků pro všechny testované systémy

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CF - Physical chemistry and theoretical chemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2005

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Chemico-Biological Interactions

  • ISSN

    0009-2797

  • e-ISSN

  • Volume of the periodical

  • Issue of the periodical within the volume

    157-158

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    2

  • Pages from-to

    387-388

  • UT code for WoS article

  • EID of the result in the Scopus database