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Proteins are chains of amino acids, and these chains have an Nitrogen-terminus and a Carbon-terminus. The Nitrogen-terminus is the end of the protein that has a nitrogen, which is available for bonding with a free carbon of another amino acid. The carbon-terminus is the end of the protein that has a carbon which is available to bond with a free nitrogen of another amino acid.
pepsin and trypsin are classified as proteins
Pepsin and trypsin both are protein digesting enzymes.
The optimal pH for trypsin is 8. It is found in the small intestine and digests proteins and polypeptides there.
Fetal bovine serum (FBS) contains trypsin inhibitors that can interfere with trypsin activity. These inhibitors can bind to and inhibit trypsin, reducing its ability to cleave proteins effectively. It is important to remove or inactivate these inhibitors when using trypsin for cell culture experiments.
serum is going to stop the action of trypsin, because it contain the inhibitors of trypisn. Once you will inhit you can see the function of trypsin. SK
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Trypsin is an enzyme that is produced in the pancreas. After the human pancreas binds to a molecule of protein, auto catalysis occurs to a molecule of trypsin.
Trypsin works best at a pH level of around 7-9. It is most active in slightly alkaline conditions. Changes in pH can affect the activity and stability of trypsin.
Trypsin is one of the 3 proteolytic digestive enzymes produced in the pancreas as Trypsinogen and is activated in the Duodenum. Trypsin derives its name from the Greek word tryein- wear down + (english) pepsin -akin to.
Cell Culture
no, something else, but i can't figure out what.
Its incative form, trypsinogen, is secreted from the pancreas....