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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The answer is xylem
Explanation
Xylem transports and stores water and water-soluble nutrients in vascular plants. Phloem is responsible for transporting sugars, proteins, and other organic molecules in plants. Vascular plants are able to grow higher than other plants due to the rigidity of xylem cells, which support the plant.
<span>Answer:
Greenhouse effect; carbon cycle affect how important a particular greenhouse gas is in contributing to the greenhouse effect.</span>
<span>C. Magma is injected into surrounding rock forming an igneous intrusion.</span>
