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: conservative model
Explanation: DNA isolated after one generation produced a single band which was a higher and intermediate in density between the heavy and light Nitrogen isotopic DNA used, showing that the first generation was a hybrid DNA. This observation fit with the dispersive and semi-conservative models only. And so at this generation, the conservative model was discarded.
<h3>Answer:</h3>
According to Charles Darwin's theory of evolution by natural selection, organisms that possess heritable traits that enable them to better adapt to their environment compared with other members of their species will be more likely to survive, reproduce, and pass more of their genes on to the next generation. So, with a process called <em>Natural</em><em> </em><em>Selec</em><em>tion</em>, the species who adapts better to their environment survive for more time, until the environment change or until appear another species better to adapt than the first one
