Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Enzyme systems transducting

This increase is thought to be one of the early steps involved in so-called signal transduction and can result in the activation of enzyme systems responsible for subsequent metabolic or developmental changes. Lymphocytes show increases in intracellular calcium in response to many kinds of specific and nonspecific surface ligand binding, some of which lead to the cellular changes that we associate with an immune response. Many other classes of cells also show calcium changes in response to stimulation. [Pg.200]

Adey WR. The sequence and energies of cell membrane transductive coupling to intracellular enzyme systems. Bioengineering 1986 15 447-56. [Pg.257]

Enzyme biosensors have been described using a range of transduction elements (amper-ometry, potentiometry, optical and photo-thermal). The first biosensor was described in the literature by Clarck and Lyons (1962a) and was based on the use of glucose oxidase combined with electrochemical detection. Since then, this principle has been widely applied in biosensor development, and the enzyme systems used have been mainly oxido-reductases (e.g. tyrosinase, peroxidase and lactase) (Cass etal., 1984 Kulis and Vidziunaite, 2003), and hydrolases (choline esterases) (Andreescu etal., 2002 Nunes etal., 1998). [Pg.141]

It has been observed that the discriminatory capabilities of human olfaction are tremendous It was estimated that an untrained person could differentiate up to ten million odors, perhaps even significantly more than that. Information theory then shows that in order to encode the qualities of ten million odors in a simple binary mode (Monoosmatic components on or off, their intensity, albeit important, is in this connection disregarded) only 2h to 27 specific profiles, disregarding possible and probable redundancies, and therefore the same number of complementary receptor sites would be required. Assuming furthermore that said redundancy, in which the informational modalities of two different specific receptor sites of two different olfactory neurons are confluent in one collector cell and therefore contribute to the expression of only one monoosmatic component is indeed operational it becomes necessary to increase the total number of types of specific receptor sites to 2k-30. This means that only 2U-30 specific detector proteins are required for structure recognition in the transduction process. This compares to about UOOO enzyme systems in different stages of activity estimated to be present in a cell any time. [Pg.168]

Qiang Cui is professor of chemistry at the University ofWisconsin-Madison, USA. He is interested in developing theoretical/computational methods for the analysis of hiomolecular systems, especially concerning chemical reactions in enzymes, energy transduction in hiomolecular machines, and, more recently, interaction between biomolecules, lipids, and inorganic materials. [Pg.571]

Figure 13.5 Spatiotemporal effects of a bioautocatalytic chemical wave revealed by time-resolved mass spectrometry, (a) Investigation of a chemical wave due to "passive" transduction and a bienzymatic amplification system. (A) Experimental setup incorporating a horizontal drift cell and mass spectrometer. (B) Schematic representation of chemical wave propagation in the drift cell due to the passive and the enzyme-accelerated transduction. (b) Transduction of labeled and unlabeled ATP along the drift cell. Concentration of the C. g-ATP trigger 0 M (A) and 5 x 10 M (B). Exponential smoothing with a time constant of 4.1 s has been applied, and followed by normalization (scaling to the maximal value). The dashed line denotes the time lapse between half-maxima of the normalized curves (0.5 level) corresponding to the passive and accelerated chemical transduction 93 and 740 s in the case of the 10 and 5 x 10 iW trigger solutions, respectively [6], Adapted from Ting, H., Urban, P.L (2014) Spatiotemporal Effects of a Bioautocatalytic Chemical Wave revealed by Time-resolved Mass Spectrometry. RSCAdv. 4 2103-2108 with permission from the Royal Society of Chemistry... Figure 13.5 Spatiotemporal effects of a bioautocatalytic chemical wave revealed by time-resolved mass spectrometry, (a) Investigation of a chemical wave due to "passive" transduction and a bienzymatic amplification system. (A) Experimental setup incorporating a horizontal drift cell and mass spectrometer. (B) Schematic representation of chemical wave propagation in the drift cell due to the passive and the enzyme-accelerated transduction. (b) Transduction of labeled and unlabeled ATP along the drift cell. Concentration of the C. g-ATP trigger 0 M (A) and 5 x 10 M (B). Exponential smoothing with a time constant of 4.1 s has been applied, and followed by normalization (scaling to the maximal value). The dashed line denotes the time lapse between half-maxima of the normalized curves (0.5 level) corresponding to the passive and accelerated chemical transduction 93 and 740 s in the case of the 10 and 5 x 10 iW trigger solutions, respectively [6], Adapted from Ting, H., Urban, P.L (2014) Spatiotemporal Effects of a Bioautocatalytic Chemical Wave revealed by Time-resolved Mass Spectrometry. RSCAdv. 4 2103-2108 with permission from the Royal Society of Chemistry...
Most biological reactions fall into the categories of first-order or second-order reactions, and we will discuss these in more detail below. In certain situations the rate of reaction is independent of reaction concentration hence the rate equation is simply v = k. Such reactions are said to be zero order. Systems for which the reaction rate can reach a maximum value under saturating reactant conditions become zero ordered at high reactant concentrations. Examples of such systems include enzyme-catalyzed reactions, receptor-ligand induced signal transduction, and cellular activated transport systems. Recall from Chapter 2, for example, that when [S] Ku for an enzyme-catalyzed reaction, the velocity is essentially constant and close to the value of Vmax. Under these substrate concentration conditions the enzyme reaction will appear to be zero order in the substrate. [Pg.252]

Other enzymes present in myelin include those involved in phosphoinositide metabolism phosphatidylinositol kinase, diphosphoinositide kinase, the corresponding phosphatases and diglyceride kinases. These are of interest because of the high concentration of polyphosphoinositides of myelin and the rapid turnover of their phosphate groups. This area of research has expanded towards characterization of signal transduction system(s), with evidence of G proteins and phospholipases C and D in myelin. [Pg.67]

Several protein assemblies have successfully been fabricated on the solid surfaces sifter the bioinformation transduction. These include the following molecular systems molecularly interfaced redox enzymes on the electrode surfaces, calmodulin / protein hybrides, and ordered antibody array on protein A. These protein assemblies find a wider application in various fields such as biosensors, bioreactors, and intelligent materials. [Pg.364]

Eukaryotic ABC transport system Phosphotransferase system (PTS) Ion-coupled transport system Signal Transduction Two-component system Bacterial chemotaxis MAPK signaling pathway Second messenger signaling pathway Ligand-Receptor Interaction G-protein-coupled receptors Ion-channel-linked receptors Cytokine receptors Molecular Assembly Ribosome assembly Flagellar assembly Enzyme assembly... [Pg.388]


See other pages where Enzyme systems transducting is mentioned: [Pg.518]    [Pg.8]    [Pg.156]    [Pg.8]    [Pg.49]    [Pg.357]    [Pg.1425]    [Pg.84]    [Pg.88]    [Pg.67]    [Pg.59]    [Pg.103]    [Pg.17]    [Pg.386]    [Pg.179]    [Pg.172]    [Pg.126]    [Pg.375]    [Pg.10]    [Pg.1184]    [Pg.1184]    [Pg.183]    [Pg.118]    [Pg.181]    [Pg.167]    [Pg.297]    [Pg.390]    [Pg.140]    [Pg.62]    [Pg.291]    [Pg.577]    [Pg.338]    [Pg.184]    [Pg.265]    [Pg.257]    [Pg.239]    [Pg.224]    [Pg.81]    [Pg.123]    [Pg.148]   
See also in sourсe #XX -- [ Pg.103 ]




SEARCH



Enzyme systems

© 2024 chempedia.info