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:glassy sweeper and squirrelfish
Explanation:neither are spotted and both have eyes on the sides of their head
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The breathing process occurs as follows: Inhalation increases the volume of the lungs, which reduces internal pressure and causes air to enter. Then the exhalation makes the opposite process. Gaseous exchanges occur in the lung alveoli and are responsible for eliminating the gases we do not need and preparing the oxygen to be spread throughout the body.
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The uterine lining of the female's uterine cycle is shed during the menstrual phase. Menstrual cycle is a reoccurring cycle which begins at menarche and ends at menopause. During menstrual cycle, the endometrial lining prepares for pregnancy.
