Uhm u should know its by pollen thats transferred by bees so asexually>
The answer that best fits the description above is the hormone GLUCOCORTICOID. This was according to Hans Selye, an Austrian-Canadian endocrinologist. According to him, ill health induced by exposure of chronic stress is due to the secretion of the hormone glucocorticoid.
Answer:
The last one
Explanation:
They are both found in the middle and everything else is false
This is a type III hypersensitivity reaction mediated by immune complex deposits. Immune complexes are antigen-antibody (commonly IgG) complexes that are soluble and prone to deposition in multiple organs. Once immune complexes are deposited in an organ, neutrophils and macrophages will then attack the organ causing organ damage and eventually failure. Type III hypersensitivity reactions are characteristic in SLE and other autoimmune diseases such as rheumatoid arthritis, etc.
Other types are type I hypersensitivity which are mediated by mast cells and histamine with the involvement of IgE and this commonly happens in allergic reactions. Type II hypersensitivity is cytotoxic hypersensitivity wherein antibodies directly attack organs (not forming immune complexes). Type IV hypersensitivity (or cell-mediated toxicity) involves T-lymphocytes. This is a delayed type of hypersensitivity exemplified by reactions from <em>M. tuberculosis</em> bacilli in tuberculous disease.
Answer:
The options A, B, and D are all valid.
Explanation:
- The reason is that some proteins require molecular chaperones if they are to fold properly within the environment of the cell. In the absence of chaperones, a partially folded polypeptide chain has exposed amino acids that can form non-covalent bonds with other regions of the protein itself and with other proteins, thus causing nonspecific aggregation of proteins.
- The option A) is correct because the protein you are expressing in bacteria is being made in large quantities, it is possible that there are not enough chaperone molecules in the bacterium to fold the protein. Expressing the protein at lower levels might increase the amount of properly folded protein.
- The option B) is correct as urea should solubilize the protein and completely unfold it. Removing the urea slowly and gradually often allows the protein to refold. Presumably, under less crowded conditions, the protein should be able to refold into its proper conformation.
- The option C) is not correct as treating the aggregate with a protease, which cleaves peptide bonds, will probably solubilize the protein by trimming it into pieces that do not interact as strongly with one another; however, chopping up the protein will also destroy its enzymatic activity.
- The option D) is correct because overexpressing chaperone proteins might increase the amount of properly folded protein.
- The option E) is not correct as heating can lead to the partial denaturation and aggregation of proteins to form a solid gelatinous mass, as when cooking an egg white, and rarely helps solubilize proteins.
