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.
To learn more about Chymotrypsin visit:
brainly.com/question/13638833
#SPJ4
Answer:
B
Explanation:
Food goes to the stomach and then both intestines
Two centrioles are found in mitosis
<span>C) secrete enzymes that kill bacteria</span>
Answer:
going through Cytokenesis.
Explanation:
This is the process which climax cells division in plans and animals where the cells cytoplasm divides and two new daughter cells are formed. it occurs both in plants and animals but in different forms.
The point of initiation of cytokinesis is determined by the mitotic spindles and basically Cytokineses marked the beginning of new generation of cells.
it occurs in 4 stages which are initiation, contraction, stage of insertions of the membrane and completion of division. It is the contraction of the membrane and the eventual formation of the two daughter cells that resulted in fig -8- shaped under microscope.