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<span>Microfilaments (actin) are important for
A.
cell movement</span>
The alpine biome is one of the coldest biomes on the planet, it is generally because of the high altitudes. The summer temperature varies in between -12 to 10 degree Celsius, and the average precipitation in the biome is about 30 cm in a year.
The animals living in the region, adapt to the cold by migrating to warmer regions, hibernating, or insulating their bodies with the help of fat and fur layers. Their bodies seem to possess shorter tails, legs, and ears, in order to minimize the loss of heat.
One of the animals living in the alpine biome is the wild yak, the animal has adapted to the biome with the help of dense and wooly coats, specially amended feet, horns to dig for food, and if necessary does the migration in winter times to the warmer regions.
Livestock candidates should be chosen based on the patient's preference as there could be organ rejection is an unbiased argument.
<h3>What is an Unbiased argument?</h3>
This type of argument shows the reader both sides and bids the reader decide.
The other options tends to support an animal which makes them biased but option D doesn't and has a credible reason which is why it's the most appropriate choice.
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Fructose-1,6-bisphosphate is a feedforward <u>allosteric</u> activator of liver pyruvate kinase.
<h3>What is the role of fructose 1/6-Bisphosphate?</h3>
A crucial enzyme in gluconeogenesis is fructose 1,6-bisphosphatase (FBPase). It is a possible target for drugs used to treat type II diabetes. Additionally, the protein is linked to a rare genetic metabolic disorder, and certain cancer cells lack the activity of the enzyme FBPase, which encourages glycolysis and aids in the Warburg effect.
The following reaction is catalyzed by FBPase. The enzyme is controlled allosterically by several small molecules, including AMP and fructose-2,6-phosphate, which are negative regulators, and ATP, which is a positive regulator. Pyruvate kinase activity is activated when FBP attaches to the allosteric binding site on domain C of the enzyme. This conformational shift is brought on by a change in the enzyme's structure.
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