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 long bones are those that are longer than they are wide.
They are one of five types of bones long, short, flat, irregular and sesamoid.
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<u>Please </u><u>mark </u><u>BRAINLIEST</u></h2>
Explanation:
Like carbon, nitrogen has its own biogeochemical cycle, circulating through the atmosphere, lithosphere, and hydrosphere (Figure 5). ... In this symbiotic association, the bacteria become encased in nodules that grow on the roots of plants, through which nitrogen that has been fixed by the resident bacteria is obtained.
