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:
This question is asking to fill in the blank spaces with the correct terms. The correct terms to the four blank spaces are:
1) GEL
2) DYE
3) DNA MARKER
4) LID
Explanation:
This question is describing the Gel electrophoresis technique which is used to separate DNA fragments using electric current. The DNA fragments of different sizes migrate through a GEL which serves as the matrix made from Agarose.
In order to physically see the samples that we put in the gel, we first have to add DYE to each sample of DNA. After loading the samples to be separated, a substance made up of DNA fragments of known sizes referred to as DNA MARKER, which acts as the standard curve in a tube is used.
Before running the gel, it's important to make sure that there is LID covering the gel in the gel rig. This will make sure that the electrical current runs through the gel and the gel stays cool.
Answer: proteins
Explanation:
The myofibril proteins are organized into filaments of varying sizes thick and thin and is called myofilaments.
Answer:
Interpreted for the first answer and for the second answer is instincts and reflexes.
Explanation:
