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:
A. BY, or YB
Explanation:
This question is depicting a phenomenon in inheritance called CODOMINANCE, which is a type of non-mendelian inheritance in which two alleles of a gene both express themselves in that gene. In this question, the allele for blue color (B) is codominant with the allele for yellow color (Y).
This means that an individual that has a blue phenotype will possess the genotype BB while an individual that has a yellow phenotype will possess the genotype YY. Hence, in an heterozygous state in which both alleles combine to produce a simultaneous blue and yellow phenotype, the genotype will be BY or YB.
Answer:
two, phospholipids, non polar, tails, polar, heads.
Explanation:
This is just basically illustrating one of the components of the lipid bilayer memebrane. The membrane is made up of two lipid layers with the polar head groups facing either the cytosol or the outer surroundings while the non polar tails facing each other. Such that this bilayer act as a barrier between the cytosol of the cell/organelle eg endoplasmic reticulum and the outer surroundings.
