Chinese and English instructions of trypsin

Enzymatic Reaction：

Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains (Brown and Wold 1973). The enzyme in excreted by the pancreas and takes part in the digestion of food proteins and other biological processes. Trypsin is a medium-sized globular protein and is produced as an inactive proenzyme, trypsinogen (Chen et al. 2009).

Specificity:

Trypsin cleaves peptides on the C-terminal side of lysine and arginine amino acid residues. If a proline residue is on the carboxyl side of the cleavage site, the cleavage will not occur. If an acidic residue is on either side of the cleavage site, the rate of hydrolysis has been shown to be slower.

Applications:

Tissue dissociation, especially when combined with other enzymes such as collagenase, and elastase

Cell harvesting by “trypsinization”

Mitochondria isolation

in vitro studies of proteins

Removing monolayers of cells from plastic and glass

Various hemagglutination procedures

Sample preparation for flow cytometric DNA analysis

Tryptic mapping

Fingerprinting and sequencing work

Environmental monitoring

Reduction of cell density in tissue culture

Subculturing cells

Cleavage fusion proteins

Generating glycopeptides from purified glycoproteins

AI Meijie Worthington Trypsin specificity ：

Trypsin cleaves amino acid residues of lysine and arginine  C  Terminal peptide . If the proline residue is located on the carboxyl side of the cleavage site , Cutting will not occur . If the acidic residue is located on either side of the cleavage site , The hydrolysis rate has been shown to be slow .

Research on trypsin ：

Cell separation optimization system

Chymotrypsin

Collagenase

Deoxyribonuclease  I

Endoprotease Lys-C

Hepatocyte isolation system

Hyaluronidase

Neonatal cardiomyocyte isolation system

Neutral protease （ Dispersing enzyme ）

Papain dissociation system

protease K

Trypsin inhibitor