GENERAL HISTOLOGY

Detailed explanation-1: -The endopeptidases cleave proteins in the middle of their chains with specificity. Trypsin, for example, cleaves the peptide bonds in which basic amino acids (lysine and arginine) contribute the carboxyl group. The carboxypeptidases cleave single amino acids off the free carboxyl ends of proteins.

Detailed explanation-2: -Here enzymes like trypsin, chymotrypsin, elastase, carboxypeptidase, and aminopeptidase convert protein molecules into amino acids, dipeptides, and tripeptides.

Detailed explanation-3: -Thus, trypsin only cleaves the peptide bonds after (on the C-terminal side of) the basic amino acids lysine and arginine while chymotrypsin prefers cleaving after large hydrophobic amino acids such as phenylalanine, tyrosine and tryptophan, and also leucine and methionine (Fig. 2).

Detailed explanation-4: -In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into smaller peptides. The peptide products are then further hydrolyzed into amino acids via other proteases, rendering them available for absorption into the blood stream.

Detailed explanation-5: -Trypsin, which is also referred to as a proteinase, goes to work with two other proteinases called pepsin and chymotrypsin to break down protein from food into amino acids. Amino acids are building blocks of protein and they are used in the body for many functions, including: Producing hormones.