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:
Spongy or cancellous tissue – the porous, honeycombed material found inside most bones, which allows the bone to be strong yet lightweight.
Answer:
B Asexual reproduction
Explanation:
Asexual reproduction only requires one parent. The offspring is essentially a clone of the parent and while becoming identical will decrease genetic variation
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Answer:
the sampling method because it involves continuing the total of numbers or organism.
The respiratory system contains the lungs, so the answer is C. Hope this helps.
