Answer:
d and b
Explanation:
I have done middle school science.
In immunology two types of immune response are described depending on whether there is prior contact with the antigen.
• At this first contact, only lymphocytes with receptors specific to the antigen in question are stimulated and lead to the production of antibodies capable of neutralizing it. The lymphocytes capable of recognizing a specific antigen are very few and the production of antibodies - of low intensity and limited duration - is detectable only after a period of latency of several days. This is called the primary response. The specificity of the resulting seropositivity, however, makes it possible to detect contamination (seroconversion).
• Upon re-contact with an antigen that has already triggered a primary response, specific antibody production is found to increase rapidly after a short latency period. The secretion of IgG then reaches levels much higher than those observed during the primary response, while that of IgM is of the same order. This early and intense response, called secondary response, most often results in the destruction of infectious agents before any clinical sign.
• Many centuries before the discovery of microbes, it was noted that people who developed a contagious disease without death were then specifically immunized against the disease, without being protected against others.
• The ability to react appropriately to an already received stimulus supposes the existence of a memory. The immune memory is based on the existence of memory B and T lymphocytes, resulting from the clonal expansion due to the first contact with the antigen. Their lifespan is significantly higher than that of other lymphocytes and their high reactivity gives its rapid and intense character to the secondary response.
Some proteins do indeed need assistance during the folding process. the general term used for the proteins that help other proteins fold is Chaperones.
<h3>What are Chaperones?</h3>
- Chaperones are proteins that help big proteins or macromolecular protein complexes fold or unfold conformationally. There are different groups of molecular chaperones, all of which have the same purpose: to help big proteins fold properly during or after synthesis as well as following partial denaturation.
- Protein translocation for proteolysis involves chaperones as well. The bulk of molecular chaperones aid in protein folding by binding to and stabilizing folding intermediates up until the polypeptide chain is entirely translated, rather than providing any steric information for protein folding.
- Based on their target proteins and location, chaperones have different unique modes of operation.
Learn more about the Protein folding with the help of the given link:
brainly.com/question/28421475
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Answer:
Filip's medical report, diagnosed with Alzhaimer's, may reveal a diminished production of acethylcholine.
Explanation:
Alzhaimer's disease is a neurodegenerative condition that causes immediate memory loss, behavioral changes and cognitive impairment, due to neuronal alterations and atrophy.
The neurotransmitter acetylcholine —related to neuronal transmission and body movement— may experience a decrease in its production leading to Alzheimer's, according to the cholinergic hypothesis.
Many therapies and treatments at present are based on the use of drugs to correct the acetylcholine deficit.
Regarding other options:
- <em>Dopamine: alteration or deficit is related to Parkinson's disease.</em>
- <em>Gamma aminobutyric acid (GABA): deficiency is not common and is related to a type of congenital and infantile neuropathy.
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- <em>Serotonin: deficit of this neurotransmitter can lead to depression and psychological disorders.</em>
Answer:assuming it is LiAlSi2O6, you have lithium, aluminum, silicon, and oxygen. It’s difficult to tell with all of the letters capitalized. Only the first letter of the atom should be capitalized. A capital I is iodine.
Explanation:
