Answer:
Mixed inhibition refers to the combination of two reversible types of enzyme inhibition, competitive inhibition and non-competitive inhibition. The term mixed is used when the inhibitor can bind both the free enzyme and the enzyme-substrate complex. In mixed inhibition the inhibitor is in a different place from the active site where the substrate is found.
Mathematically, mixed inhibition occurs when both alpha and alpha-prime factors (introduced in the Michaelis-Menten equation representing competitive and non-competitive inhibition respectively) are present (they are larger than unity).
In a special case of mixed inhibition, the alpha and alpha-prime factors are the same, then non-competitive inhibition occurs.
With this type of inhibition Km depends on the affinity of the inhibitor to join E or ES and Vmax decreases.
Enzymatic inhibitors are molecules that bind enzymes and decrease their activity. Since blocking an enzyme can kill a pathogen or correct a metabolic imbalance, many medications act as enzyme inhibitors. They are also used as herbicides and pesticides. However, not all molecules that bind to enzymes are inhibitors; Enzymatic activators bind to enzymes and increase their activity.
The binding of an inhibitor can prevent the substrate from entering the active site of the enzyme and / or hinder the enzyme from catalyzing its corresponding reaction. The inhibitor binding may be reversible or irreversible. Normally, irreversible inhibitors react with the enzyme covalently and modify their chemical structure to the level of essential residues necessary for enzymatic activity. In contrast, reversible inhibitors bind to the enzyme in a non-covalent manner, resulting in different types of inhibitions, determined whether the inhibitor binds to the enzyme, the enzyme-substrate complex or both.
Many medications are enzymatic inhibitors, so their discovery and improvement is an active field of research in biochemistry and pharmacology. The validity of a medicinal enzyme inhibitor is usually determined by its specificity (its inability to bind to other proteins) and its potency (its dissociation constant, which indicates the concentration necessary to inhibit an enzyme). A high specificity and potency ensures that the medication will have few side effects and therefore a low toxicity.
b. Decrease peripheral resistance
c. Vasodilation
d. Decrease salt intake
e. Decrease blood volume
f. Vasoconstriction
g. Increase peripheral resistance
h. Increase salt intake
i. Increase blood volume
j. Increase water reabsorption
Answer:
a. Decrease water reabsorption: decrease blood pressure.
b. Decrease peripheral resistance: decrease blood pressure
c. Vasodilation: decrease blood pressure
d. Decrease salt intake: decrease blood pressure
e. Decrease blood volume: decrease blood pressure
f. Vasoconstriction: increase blood pressure
g. Increase peripheral resistance: increase blood pressure
h. Increase salt intake: increase blood pressure
i. Increase blood volume: increase blood pressure
j. Increase water reabsorption: increase blood pressure
Explanation:
Administration of basic life support is necessary when put in htis scenario.
The first thing to do is to open the airway with the head-tilt/chin-lift maneuver, look-listen-feel for breathing, and if the child is not breathing normally give 2 rescue breathes.
Answer:
during external respiration
Explanation:
Oxyhemoglobin is a type of hemoglobin carrying oxygen which is bright red in color. In the blood, it's major function is to carry oxygen molecules throughout the body.
Oxyhemoglobin is formed during external respiration. External respiration also known as breathing occurs in the lung. During external respiration, there is an exchange of oxygen and carbon-dioxide between the cells of the body and blood vessels. During breathing, oxygen diffuses into the blood, the oxygen then binds with heme in the hemoglobin found in erythrocytes to form oxyhemoglobin.
Answer:
during external respiration
Explanation:
Oxyhemoglobin is a protein formed when hemoglobin is combined with an oxygen molecule during lung respiration, also called external respiration. Its function is to transport oxygen throughout the body.
External breathing is performed when we breathe in oxygen into the body. This oxygen will be used for cells to perform cellular respiration that will be responsible for exhaling carbon dioxide out of our body.
Answer:
To view prokaryotes with the compound microscope, you must use an oil-immersion lens (100x objective).
Answer:
UUU
Explanation:
A codon is a sequence of three nucleotide bases in a mRNA molecule that specifies an amino acid. During the process of translation, the mRNA strand is read in a group of three nucleotides at a time. A type of RNA called transfer RNA (tRNA) posseses in its structure another group of triplet nucleotides called ANTICODON, which is complementary to the sequence of bases in the mRNA codon.
The tRNA anticodon recognizes and binds to the particular mRNA codon it is complementary to in order to carry the amino acid it specifies to the growing polypeptide chain In this case, the mRNA codon reads AAA. This means that the anticodon on the tRNA that will bind to this codon is UUU.
Answer:
1st one
Explanation:
B. Thiamine pyrophosphate
C. Biotin
D. FAD
Answer: Option B.
Thiamine pyrophosphate.
Explanation:
Pyruvate dehydrogenase is an enzyme that catalyses the oxidative decarboxylation of pyruvate to acetyl coA , NADH and CO2. Pyruvate dehydrogenase uses NAD, biotin, FAD and lipoic acid.
Thiamine pyrophosphate is not a cofactor for pyruvate dehydrogenase . It is a cofactor in living systems. Thiamine pyrophosphate is a coenzyme that function in carbohydrates, Amino acids and lipids metabolism.
Biotin is not a cofactor in the reaction catalyzed by pyruvate dehydrogenase. NAD+, Thiamine pyrophosphate, and FAD do function as cofactors in this reaction.
The cofactors used in the reaction catalyzed by pyruvate dehydrogenase are NAD+, Thiamine pyrophosphate, and FAD. The compound that is not used as a cofactor in this reaction is Biotin. Biotin functions as a cofactor for carboxylase enzymes, and it is involved in fatty acid synthesis and gluconeogenesis but not in the process involving pyruvate dehydrogenase.
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