Trypsin

trypticanti-tryptictrypsin serine proteases
Trypsin is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins.wikipedia
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Trypsinogen

Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated.
Trypsinogen (EC 3.4.23.18/20/21/23/24/26) is the precursor form or zymogen of trypsin, a digestive enzyme.

Small intestine

small bowelsmall intestinessmall
Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated.

Trypsinization

trypsinisationtrypsinized
The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.
Trypsinization is the process of cell dissociation using trypsin, a proteolytic enzyme which breaks down proteins, to dissociate adherent cells from the vessel in which they are being cultured.

Proteolysis

proteolyticprotein degradationpolyprotein
The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.
Proteolysis of the zymogen yields an active protein; for example, when trypsinogen is cleaved to form trypsin, a slight rearrangement of the protein structure that completes the active site of the protease occurs, thereby activating the protein.

Pancreas

pancreaticexocrine pancreaspancreatic development
Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated.

Enteropeptidase

enterokinase
Once in the small intestine, the enzyme enteropeptidase activates trypsinogen into trypsin by proteolytic cleavage.
Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes.

Catalytic triad

triadactive sitecatalytic tryad
These enzymes contain a catalytic triad consisting of histidine-57, aspartate-102, and serine-195.
The enzymes trypsin and chymotrypsin were first purified in the 1930s.

Protease

proteasespeptidaseproteinase
Once in the small intestine, the enzyme enteropeptidase activates trypsinogen into trypsin by proteolytic cleavage.
Each family may contain many hundreds of related proteases (e.g. trypsin, elastase, thrombin and streptogrisin within the S1 family).

Wilhelm Kühne

Wilhelm KuhneKühne, Wilhelm (Willy) FriedrichWilly Kuhne
Trypsin was discovered in 1876 by Wilhelm Kühne and was named from the Ancient Greek word for rubbing since it was first isolated by rubbing the pancreas with glycerin.
In 1876, he discovered the protein-digesting enzyme trypsin.

Duodenum

duodenaldodecadactylumduodenal cap
In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into smaller peptides.
These cause the liver and gall bladder to release bile, and the pancreas to release bicarbonate and digestive enzymes such as trypsin, lipase and amylase into the duodenum as they are needed.

Serine

SerL-serineS
These enzymes contain a catalytic triad consisting of histidine-57, aspartate-102, and serine-195.
It has been shown to occur in the active sites of chymotrypsin, trypsin, and many other enzymes.

Chymotrypsin

Alpha Chymaralpha-chymotrypsinbovine alpha-chymotrypsin
The activity of trypsin is not affected by the enzyme inhibitor tosyl phenylalanyl chloromethyl ketone, TPCK, which deactivates chymotrypsin.
It is activated in the presence of trypsin.

Enzyme inhibitor

inhibitorinhibitioninhibitors
The activity of trypsin is not affected by the enzyme inhibitor tosyl phenylalanyl chloromethyl ketone, TPCK, which deactivates chymotrypsin.
In a complementary technique, peptide mass fingerprinting involves digestion of the native and modified protein with a protease such as trypsin.

Endopeptidase

endopeptidasesendoproteaseendopeptidase clp
Trypsin is considered an endopeptidase, i.e., the cleavage occurs within the polypeptide chain rather than at the terminal amino acids located at the ends of polypeptides.

Enzyme kinetics

kineticsping-pong mechanismenzyme kinetic
The enzymatic reaction that trypsin catalyzes is thermodynamically favorable, but requires significant activation energy (it is "kinetically unfavorable").
Enzymes with ping–pong mechanisms include some oxidoreductases such as thioredoxin peroxidase, transferases such as acylneuraminate cytidylyltransferase and serine proteases such as trypsin and chymotrypsin.

PRSS3

protease, serine, 3 (mesotrypsin)trypsin-3
This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases.

Aprotinin

BPTIbovine pancreatic trypsin inhibitorTrasylol
To prevent the action of active trypsin in the pancreas, which can be highly damaging, inhibitors such as BPTI and SPINK1 in the pancreas and α1-antitrypsin in the serum are present as part of the defense against its inappropriate activation.
The drug aprotinin (Trasylol, previously Bayer and now Nordic Group pharmaceuticals), is a small protein bovine pancreatic trypsin inhibitor (BPTI), or basic trypsin inhibitor of bovine pancreas, which is an antifibrinolytic molecule that inhibits trypsin and related proteolytic enzymes.

PRSS2

protease, serine, 2 (trypsin 2)trypsin-2
This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases.

Alpha-1 antitrypsin

alpha 1-antitrypsinα 1 -antitrypsinα1-antitrypsin
To prevent the action of active trypsin in the pancreas, which can be highly damaging, inhibitors such as BPTI and SPINK1 in the pancreas and α1-antitrypsin in the serum are present as part of the defense against its inappropriate activation.
A protease inhibitor, it is also known as alpha 1 –proteinase inhibitor (A1PI) or alpha 1 -antiproteinase (A1AP) because it inhibits various proteases (not just trypsin).

Trypsin 1

PRSS1cationic trypsinogenprotease, serine, 1 (trypsin 1)
This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases.

Casein

sodium caseinatemicellar caseincasein protein
Trypsin can be used to break down casein in breast milk.
The enzyme trypsin can hydrolyze a phosphate-containing peptone.

Tosyl phenylalanyl chloromethyl ketone

tosylphenylalanyl chloromethyl ketoneTPCK
The activity of trypsin is not affected by the enzyme inhibitor tosyl phenylalanyl chloromethyl ketone, TPCK, which deactivates chymotrypsin.
It does not inhibit trypsin or zymogens.

Mass spectrometry

mass spectrometerMSmass spectrometric
This is important because, in some applications, like mass spectrometry, the specificity of cleavage is important.
In the second, proteins are enzymatically digested into smaller peptides using proteases such as trypsin or pepsin, either in solution or in gel after electrophoretic separation.

In-gel digestion

in gel
Trypsin is commonly used in biological research during proteomics experiments to digest proteins into peptides for mass spectrometry analysis, e.g. in-gel digestion.
The serine protease trypsin is the most common enzyme used in protein analytics.

Zymogen

proenzymezymogenspro-enzyme
Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated.