Chymotrypsin is used for polypeptide cleavage on the C side of Trp, Tyr or Phe.
<h3>What is Chymotrypsin?</h3>
Other proteins' aromatic C-terminal amino acids are hydrolyzed by it using an active serine residue. The protease enzyme chymotrypsin cleaves peptide chains at the C-terminal phenylalanine (F), tryptophan (W), and tyrosine (Y) residues.
Since the 1960s, chymotrypsin has been used in clinical settings as an oral proteolytic enzyme preparation. In comparison to a few other enzyme preparations currently on the market, it offers better inflammatory symptom relief and supports a quicker recovery from acute tissue injury.
The inactive monomeric protein chymotrypsinogen, which is produced and secreted by mammalian pancreas, is broken down into chymotrypsin by cleavage of several peptide bonds. As a result, three different polypeptide chains that make up the active enzyme were created.
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Answer:
mitosis: It is a process by which the duplicated genome in cell is separated into halves that are in nature.
It occur in three phases: interphases, karyokines and cytokinesis.
Cytokinesis: It is a process where the cytoplasm of cell divided two "daughter" cells.
It occur through two processes: in animals, in eukaryotic cell and one in plant cell.
Answer:
All this combination of reactions is summarized in that the bacteria reduced nitrate, that is, they added protons to said compound, giving nitrite as a product.
By promoting the appearance of nitrite and that it increases in its concentrations when the zinc dust is thrown away, it becomes reddish since there was a change in pH, that is, the medium was acidified.
Explanation:
Some bacteria take nitrate as a source and end up generating an oxide reduction reaction that gives nitrite as a product, if this reaction advances in a chain, that is, the nitrite is reduced after the nitrate, the product in the future would be ammonia
Answer:
its b sunlight
Explanation: because why would a plant grow according to pressure gravity or touch.
