Answer:
d. it's not a fossil fuel
Answer:
a. Acetyl CoA carboxylase
Explanation:
Much of the fatty acids used by the body is supplied by the diet, excessive amounts of carbohydrates and protein obtained from the diet can be converted to fatty acids and stored as triglycerides. Fatty acid synthesis occurs mainly in the liver and mammary glands, and to a lesser extent in adipose tissue and kidney, the process incorporates acetyl CoA carbons into the forming fatty acid chain using ATP and NADPH.
The acetyl portion of acetyl CoA is transported to cytosol as citrate, produced by condensation of oxaloacetate and acetyl CoA, the first reaction of the citric acid cycle, this occurs when the concentration of mitochondrial citrate is high, observed when there is a high concentration of ATP and isocitrate dehydrogenase is inhibited. The increase of citrate and ATP favors the synthesis of fatty acids, since this pathway needs both. Acetyl CoA should be converted to malonyl CoA. Carboxylation is catalyzed by acetyl CoA carboxylase and requires ATP, this reaction is the regulated step in fatty acid synthesis: it is inactivated by products, malonyl CoA and palmitoyl CoA, and activated by citrate, another regulatory mechanism is reversible phosphorylation of enzyme, which makes it inactive due to the presence of adrenaline / glucagon
C. mRNA detaches and moves to the ribosomes.
The structure of a typical antibody molecule
Antibodies are the secreted form of the B-cell receptor. An antibody is identical to the B-cell receptor of the cell that secretes it except for a small portion of the C-terminus of the heavy-chain constant region. In the case of the B-cell receptor the C-terminus is a hydrophobic membrane-anchoring sequence, and in the case of antibody it is a hydrophilic sequence that allows secretion. Since they are soluble, and secreted in large quantities, antibodies are easily obtainable and easily studied. For this reason, most of what we know about the B-cell receptor comes from the study of antibodies.
Antibody molecules are roughly Y-shaped molecules consisting of three equal-sized portions, loosely connected by a flexible tether. Three schematic representations of antibody structure, which has been determined by X-ray crystallography, are shown in Fig. 3.1. The aim of this part of the chapter is to explain how this structure is formed and how it allows antibody molecules to carry out their dual tasks—binding on the one hand to a wide variety of antigens, and on the other hand to a limited number of effector molecules and cells. As we will see, each of these tasks is carried out by separable parts of the molecule. The two arms of the Y end in regions that vary between different antibody molecules, the V regions. These are involved in antigen binding, whereas the stem of the Y, or the C region, is far less variable and is the part that interacts with effector cells and molecules.
Answer:
True
Explanation:
Truly, the typical X shaped chromosomes is the result of DNA replication. When the DNA has replicated, it then condenses and coil into the X-shaped of the chromosome. This then implies that replicated chromosomes take the X-shaped structures seen under a microscope.
When this replication occurs, the chromosome is made of two structures that are identical. They are known as the sister chromatids. These chromatids are actually joined at the centromere.
