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djverab [1.8K]
3 years ago
10

Need people to talk to and maybe a bit of role play but mainly talk

Biology
2 answers:
slamgirl [31]3 years ago
8 0

yo you know how to delete questions?

alexandr402 [8]3 years ago
4 0

Answer:

what do you want to talk about?

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8_murik_8 [283]

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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Below is a chart of the embryo development of many different organisms, starting with a fish and ending with a human.
Goryan [66]
They have the same bone structure
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