Answer: a. True
Explanation:
Glomerular filtrate is formed by the difference in force of hydrostatic and osmotic pressure. This physical force involves:
Bowman's capsule hydrostatic pressure: This includes the pressure that develops in the Bowman's capsule against the fluid to be filtrated expelled out by the glomerulus.
Glomerular hydrostatic pressure: The glomerulus is the main site of production of filtrate. It is higher than the average blood capillary hydrostatic pressure. It allows the water and solute molecules to be filtrated out of the plasma membrane.
Colloid osmotic pressure: The osmotic pressure which is generated by the large molecules is the colloid osmotic pressure. It is created by the plasma proteins. This pressure draws water from the glomerulus.
Answer:
The correct answer is "both Cdc6 and Cdt1"
Explanation:
The replisome is a complex molecular system that allows for the replication of DNA in yeast. There are multiple genes that participate in the replisome function, however if a researcher finds out that a yeast strain fails to properly form replisomes it is very likely that the genes that might be mutated are both Cdc6 and Cdt1. Cdc6 and ORC are the genes that send the signal to the yeast to start the replisome formation, and Cdt1 is a DNA replication factor that if it is mutated it could cause that yeast is not able to form the replisome.
Answer:
b. to amplify the signal
Explanation:
A multi-enzyme phosphorylation cascade is a series of signaling events where one enzyme phosphorylates to another, then this last enzyme acts to phosphorylate another protein and so successively, thereby triggering a chain reaction that leads to the phosphorylation of hundreds or even thousands of proteins. A multi-enzyme phosphorylation cascade is known to increase the number of activated (phosphorylated) proteins at each step of the signaling cascade. Phosphorylation is a posttranslational modification capable of activating proteins during long periods, thereby a phosphorylation cascade also enables the activation of multiple proteins before these proteins become inactive again.
