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The truth drug, you cannot lie while you are under its influence.
Sodium thiopental is a barbiturate; these are drugs that act on the gamma-amino butyric acid (GABAa) receptor which decrease neuronal activity. Barbiturates enhance the GABAa receptors, decreasing drastically neuronal activity. It is because of this that overdoses can be lethal. In fact many famous people have died due to overdose on barbiturate-based drugs: e.g. Elvis Presley, Marilyn Monroe, Jimmy Hendrix, and others. The A.U.M., the Japanese terrorist group that in 1995 released sarin nerve gas in the Tokyo subway, is reported to use sodium thiopental on their members to keep them loyal. It is believed that their chief chemist produced 1.7 kg of sodium thiopental.
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Sodium thiopental is very well known to moviegoers as the "truth serum". Movies such as Stormbreaker, Meet the Fockers, Kill Bill vol.2, are recent examples of Hollywood's poetic license when it comes to the use of this 'truth serum'. However, sodium thiopental was used by the CIA for many years, and was recently used against Al-Qaeda members to find out secrets within the organization. As mentioned above, it isn't actually a 'truth serum' as such, but it reduces neuronal activity making it harder and harder to think. Using the fact that it is harder for the brain to tell a lie than to tell the truth, sodium thiopental makes the subject dreamily blurt out the truth. But it does not work on people who truly believe in their lies, and therefore is not a reliable source of information.
What else can I help you with?
Is lactose a noncompetitive inhibitor?
No, lactose is not a noncompetitive inhibitor. Lactose is a sugar found in milk that can act as an inducer for the lactose operon in bacteria, but it does not act as an inhibitor in enzyme kinetics.
What inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate?
A competitive inhibitor has a structure that closely resembles the substrate, allowing it to bind to the enzyme's active site in a similar manner. This competition between the inhibitor and substrate for the active site directly affects the enzyme's ability to catalyze reactions.
What would happen if most biochemical reactions are catalyzed by the same enzyme?
If an enzyme produces too much of one substance in the organism, that substance may act as an inhibitor for the enzyme at the beginning of the pathway that produces it, causing production of the substance to slow down or stop when there is sufficient amount.
What is the opposite of a enzyme?
The opposite of an enzyme can be considered an inhibitor, which is a substance that decreases or prevents the activity of an enzyme. While enzymes catalyze biochemical reactions, inhibitors can bind to the enzyme or its substrate, effectively reducing its efficiency or halting the reaction altogether. Alternatively, one could also consider substrates as opposites in a functional sense, as they are the molecules upon which enzymes act.
Which one of the following would you predict is an allosteric inhibitor of the Krebs cycle enzyme ketoglutarate dehydrogenase?
It is likely that ATP could act as an allosteric inhibitor of ketoglutarate dehydrogenase in the Krebs cycle. High levels of ATP signal that the cell has sufficient energy, so it would make sense for ATP to inhibit an enzyme involved in generating more energy through the cycle.
How can a molecule serve as both an inhibitor and substrate in an enzyme system characterized by feedback inhibition?
In a feedback inhibition system, a molecule can act as both an inhibitor and substrate by participating in the metabolic pathway it regulates. As a substrate, it is converted into a product by an enzyme, which then can accumulate and bind to an earlier enzyme in the pathway, inhibiting its activity. This dual role helps maintain homeostasis, ensuring that the pathway is active only when needed, preventing overproduction of the end product. This regulatory mechanism allows for fine-tuning of metabolic processes based on the cell's needs.
Molecule that binds to an enzyme?
A molecule that binds to an enzyme is usually referred to as a substrate. Substrates are the molecules on which enzymes act to catalyze a biochemical reaction. Upon binding to the enzyme's active site, substrates undergo a chemical transformation to form products.
How does sodium benzoate affect salivary digestion?
Sodium benzoate, the well known food preservative has no effect whatsoever on salivary digestion because it wont act on amylase the enzyme present in saliva. But it is known for affecting pepsin and trypsin, the intestinal enzymes.
What can you say about sodium silicate as a dispersant?
Sodium silicate is commonly used as a dispersant in various applications, such as in detergents and in the paper industry. It helps to prevent particles from clumping together by keeping them dispersed in a liquid. Sodium silicate can also act as a stabilizer and corrosion inhibitor in certain formulations.
What does a competitive inhibitor bind to?
A competitive inhibitor is a molecule that binds to the active site of an enzyme, to prevent substrates entering the active site and therefore lowering the rate of reaction. Some drugs act as competitive inhibitors to control reactions in the body, and the body also releases competitive inhibitors as a means of self control. But remember that the amount of product formed is still remain the same, only the time taken increased.
Is a enzyme a protein that acts as a catalyst formed?
All Enzyme are proteins enzymes act as catalyst
What part does dopamine reuptake inhibitor act?
Inhibits the reuptake of dopamine resulting in euphoria etc
