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Biochemical switch sensitivity

In an extensive study, Okamoto and co-workers [76-86] introduced a biochemical switching device based on a cyclic enzyme system in which two enzymes share two cofactors in a cyclic manner. Cyclic enzyme systems have been used as biochemical amplitiers to improve the sensitivity of enzymatic analysis [87-89], and subsequently, this technique was introduced into biosensors [90-93], In addition, cyclic enzyme systems were also widely employed in enzymic reactors, in cases where cofactor regeneration is required [94-107], Using computer simulations, Okamoto and associates [77,80-83] investigated the characteristics of the cyclic enzyme system as a switching device, and their main model characteristics and simulation results are detailed in Table 1.1, as is a similar cyclic enzyme system introduced by Hjelmfelt et al. [109,116], which can be used as a logic element. [Pg.6]

The hybrid can be used with El, Cl, FI, FD, LSIMS, APCI, ES, and MALDI ionization/inlet systems. The nature of the hybrid leads to high sensitivity in both MS and MS/MS modes, and there is rapid switching between the two. The combination is particularly useful for biochemical and environmental analyses because of its high sensitivity and the ease of obtaining MS/MS structural information from very small amounts of material. The structural information can be controlled by operating the gas cell at high or low collision energies. [Pg.161]

Fig. 1 Molecular and biochemical basis of Friedreich s ataxia (FRDA). (a) A GAA-repeat expansion in the first intron of the FRDA gene results in decreased levels of frataxin as a result of inhibition of transcriptional elongation, (b) Alterations in mitochondrial biochemistry that are associated with reduced frataxin levels. Proposed functions for frataxin include iron binding, protection and synthesis of Fe-S clusters, providing a binding partner for ferrochetalase in heme (haem) metabolism, and providing a metabolic switch between heme metabolism and Fe-S cluster biosynthesis. In FRDA, reduction of firataxin results in lowered levels of aconitase and respiratory complexes 1,11, and 111. Cytosolic proteins that contain Fe-S clusters may also be affected. Inability to form Fe-S clusters leads to an accumulation of iron, which leads to increased free radical formation (Fenton chemistry) in these organelles. Increased free radical formation may feed back to further decrease levels of Fe-S clusters, which are known to be sensitive to oxidative stress. Fig. 1 Molecular and biochemical basis of Friedreich s ataxia (FRDA). (a) A GAA-repeat expansion in the first intron of the FRDA gene results in decreased levels of frataxin as a result of inhibition of transcriptional elongation, (b) Alterations in mitochondrial biochemistry that are associated with reduced frataxin levels. Proposed functions for frataxin include iron binding, protection and synthesis of Fe-S clusters, providing a binding partner for ferrochetalase in heme (haem) metabolism, and providing a metabolic switch between heme metabolism and Fe-S cluster biosynthesis. In FRDA, reduction of firataxin results in lowered levels of aconitase and respiratory complexes 1,11, and 111. Cytosolic proteins that contain Fe-S clusters may also be affected. Inability to form Fe-S clusters leads to an accumulation of iron, which leads to increased free radical formation (Fenton chemistry) in these organelles. Increased free radical formation may feed back to further decrease levels of Fe-S clusters, which are known to be sensitive to oxidative stress.
Then x variable plays in Zeeman s model the role of length of a fibre of the cardiac muscle while the b variable corresponds to the electrochemical control (contraction of the cardiac muscle is triggered by a biochemically generated electric impulse). A stable stationary point E may occur near the point B which is infinitely sensitive to perturbations. To transfer the system from the stable stationary point E to B, a perturbation of the system is required if E is located close to B the perturbation can be small. The mechanism of switching the heart from the state of equilibrium E (lack of heartbeat) to the state of action involves removing the system from the state E to B by way of stimulation, for example by an electric impulse. On reaching the state B the model system imitates the heartbeat — this is the trajectory BB CC E. A subsequent cycle requires the repeated stimulation at the point E. [Pg.113]

Rea instructs that several principles must be considered to demonstrate the influence of environmental chemicals on chanical sensitivity. These include total body load, adaptation, bipolarity, biochemical individuality, spreading, and switch phenomenon [15,16]. [Pg.370]

This is a pity because transport functions have clear implications for new technology. As one example, the current thrust in biosensors seeks to transplant natural transport systems into artificial sensors which could then exhibit the inherent sensitivity of the biochemical apparatus. Can this be extended to other technological goals such as molecular switches or ionic computers Possibly, but the process will be plagued with the problems of maintaining a natural" environment in an artificial... [Pg.38]


See other pages where Biochemical switch sensitivity is mentioned: [Pg.31]    [Pg.109]    [Pg.110]    [Pg.247]    [Pg.2090]    [Pg.162]    [Pg.135]    [Pg.190]    [Pg.141]    [Pg.247]    [Pg.446]    [Pg.75]    [Pg.58]    [Pg.340]    [Pg.1495]    [Pg.1130]    [Pg.458]    [Pg.316]    [Pg.176]    [Pg.393]    [Pg.396]    [Pg.109]   
See also in sourсe #XX -- [ Pg.111 ]




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Biochemical switching

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