Trypsin cleaves the peptide bond on the carboxyl side of basic amino acids such as arginine and lysine.

Trypsin in the duodenum catalyses the hydrolysis of peptide bonds so that proteins can be broken down into smaller peptides.

Trypsin () is a serine protease found in the digestive system of many vertebrates, where it hydrolyses proteins.

Trypsin is produced in the pancreas as the inactive proenzyme trypsinogen.

Trypsin is produced in the pancreas in the form of the inactive zymogen trypsinogen.

Trypsin can then function to activate additional trypsinogen ( autocatalysis ), so only a small amount of enteropeptidase is necessary to start the reaction.

Trypsin is the major primary hydrolytic protease and is secreted into the posterior midgut lumen without activation in the posterior midgut epithelium.

Trypsin is an enzyme involved in digestion, and phytates reduce the bioavailability of dietary minerals.

Trypsin, a type of peptidase, is a digestive enzyme active in the duodenum and elsewhere.

Trypsin is produced, stored and released as the inactive trypsiongen to ensure that the protein is only activated in the appropriate location.

Trypsin autocatalytic activation of trypsinogen is also a slow process due to the presence of a large negative charge on the conserved N-terminal hexapeptide of trypsinogen which repels the aspartate on the back of trypsin's specificity pocket.

Trypsin may also inactivate other trypsin by cleavage.

Involved genes may include Trypsin 1, which codes for trypsinogen, SPINK1, which codes for a trypsin inhibitor, or cystic fibrosis transmembrane conductance regulator.

* Trypsin to detect cystic fibrosis.

Seeds of Gleditsia triacanthos contain a trypsin inhibitor .< ref > Mosolov V. V., Kolosova G. V., Valueva T. A., Dronova L. A. " Trypsin inhibitor from Gleditsia triacanthos L. seeds.

For his 1939 book, Crystalline Enzymes: The Chemistry of Pepsin, Trypsin, and Bacteriophage, Northrop was awarded the Daniel Giraud Elliot Medal from the National Academy of Sciences.

X-ray crystallography | Crystal structure of Trypsin, a typical serine protease.

Trypsin can then activate other protease enzymes and catalyze the reaction pro-colipase → colipase.

Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond ( the P < sub > 1 </ sub > position ) is a tyrosine, tryptophan, or phenylalanine.

Chymotrypsin cleaves peptide bonds by attacking the unreactive carbonyl group with a powerful nucleophile, the serine 195 residue located in the active site of the enzyme, which briefly becomes covalently bonded to the substrate, forming an enzyme-substrate intermediate.

Different enzymes have different specificity for their substrate ; trypsin for example cleaves the peptide bond after a positively charge residue ( arginine and lysine ), chymotrypsin cleaves the bond after an aromatic residue ( phenylalanine, tyrosine, and tryptophan ), elastase cleaves the bond after a small non-polar residue such as alanine or glycine.

# Renin cleaves a zymogen, an inactive peptide, called angiotensinogen, converting it into angiotensin I.

Renin cleaves the peptide bond between the leucine ( Leu ) and valine ( Val ) residues on angiotensinogen, creating the ten-amino acid peptide ( des-Asp ) angiotensin I ( CAS # 9041-90-1 ).

The last residue of the intein is always an asparagine, and the amide nitrogen atom of this side chain cleaves apart the peptide bond between the intein and the C-extein, resulting in a free intein segment with a terminal cyclic imide.

Once translation is finished a signal peptidase cleaves off the short signal peptide from the nascent protein leaving the polypeptide free in the interior of the endoplasmic reticulum.

To be specific, tPA cleaves the zymogen, plasminogen at its Arg560-Val561 peptide bond, into the serine protease plasmin.

Enterokinase is produced by the mucosa of duodenum and it cleaves the peptide bond of trypsinogen after residue 15 which is a lysine.

Since trypsin also cleaves the peptide bond after an arginine or a lysine, it can cleave other trypsinogen, and the activation process therefore becomes autocatalytic.

It is formed when C1s cleaves off a small peptide fragment of C2 C2b from a membrane-bound C4b-C2a complex.

The γ secretase, which produces the C-terminal end of the Aβ peptide, cleaves within the transmembrane region of APP and can generate a number of isoforms of 36-43 amino acid residues in length.

To produce an F ( ab ') 2 fragment, IgG is digested with pepsin, which cleaves the heavy chains near the hinge region.

Papain cleaves IgG above the hinge region containing the disulfide bonds that join the heavy chains, but below the site of the disulfide bond between the light chain and heavy chain.

First, thrombin cleaves the N-terminus of the fibrinogen alpha and beta chains to fibrinopeptide A and B respectively.

* Exocellulase ( EC 3. 2. 1. 91 ) cleaves two to four units from the ends of the exposed chains produced by endocellulase, resulting in the tetrasaccharides or disaccharides, such as cellobiose.

Or it merely cleaves polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common.

A specialized enzyme, sortase, cleaves the target protein at a characteristic recognition site near the protein C-terminus, such as an LPXTG motif ( where X can be any amino acid ), then transfers the protein onto the cell wall.

However, HpaII requires that a C within that site be methylated, whereas MspI cleaves only DNA methylated at that site.

This means that trypsin predominantly cleaves proteins at the carboxyl side ( or " C-terminal side ") of the amino acids lysine and arginine except when either is bound to a N-terminal proline., although large-scale mass spectrometry data suggest cleavage occurs even with proline.

First the β-carotene 15-15 ’- monooxygenase cleaves β-carotene at the central double bond, creating an epoxide.

For to obey such a commandment would have been contrary to the nature of man, who generally cleaves to that to which he is used ; it would in those days have made the same impression as a prophet would make at present 12th Century if he called us to the service of God and told us in His name, that we should not pray to God nor fast, nor seek His help in time of trouble ; that we should serve Him in thought, and not by any action.

After mitosis, division occurs by the formation of a septum, or cell plate, that cleaves the cell at its midpoint.

* Endocellulase ( EC 3. 2. 1. 4 ) randomly cleaves internal bonds at amorphous sites that create new chain ends.

: RNase I cleaves 3 '- end of ssRNA at all dinucleotide bonds leaving a 5 '- hydroxyl, and 3 '- phosphate, via a 2 ', 3 '- cyclic monophosphate intermediate.

It is a metalloproteinase that cleaves vWF between tyrosine at position 842 and methionine at position 843 ( or 1605 – 1606 of the gene ) in the A2 domain.

For to obey such a commandment would have been contrary to the nature of man, who generally cleaves to that to which he is used ; it would in those days have made the same impression as a prophet would make at present 12th Century if he called us to the service of God and told us in His name, that we should not pray to God nor fast, nor seek His help in time of trouble ; that we should serve Him in thought, and not by any action.

When the Dicer, which has endonuclease activity against dsRNA and pre-miRNAs, cleaves a pre-miRNA stem-loop or a dsRNA, a 20-to 25-base-pair double-stranded RNA fragment is formed with a two-nucleotide 3 ' overhang at each end.

In V ( D ) J recombination, hairpin-capped double-strand breaks are created by the RAG1 / RAG2 nuclease, which cleaves the DNA at recombination signal sequences.

Viral protein A cleaves replicative form I DNA strand at the origin of replication ( ori ) and covalently attaches itself to the DNA, generating replicative form II molecule.

Papain prefers to cleave at: ( hydrophobic )-( Arg or Lys )- cleaves here -( not Val ).

He demonstrates his immense power as an ancient Seeker when he arrives late in the final battle at the Giza Necropolis, and cleaves his battleaxe clear through Mixmaster and stomps off his head, killing him and saving the human forces nearby, although soon after he is attacked and mortally wounded by Scorponok but manages to easily crush his attacker after recovering from the surprise attack ( saying he is " too old for this crap ").