Examples of 'trypsin' in a sentence
Meaning of "trypsin"
trypsin (noun) - an enzyme produced in the pancreas that helps in the digestion of proteins. It is commonly found in the digestive system of animals, including humans. Example: 'Trypsin breaks down proteins into smaller peptides during the digestion process.'
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- A digestive enzyme that cleaves peptide bonds (a serine protease)
How to use "trypsin" in a sentence
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trypsin
Trypsin then cleaves proteins to smaller polypeptides.
These are activated by trypsin in the duodenal lumen.
The trypsin is immobilized covalently on nylon spheres.
Some preparations of trypsin contain phenol red.
Trypsin inhibitors and haemagglutinin are growth inhibitors.
Enteropeptidase converts trypsinogen into a molecule of trypsin.
Trypsin cleaves after arginines and lysins.
In situ digestion by trypsin resulted in several fragments.
Trypsin specifically cleaves adjacent to basic residues.
One fraction is treated enzymatically with trypsin.
Digestion with trypsin is very dependent on temperature.
The larger protein is a powerful inhibitor of trypsin.
Trypsin is most effective on partially digested proteins.
One to two ml of additional trypsin solution is added.
Trypsin inhibitors can be isolated by numerous procedures.
See also
The enzyme was activated by incubation with trypsin.
The trypsin was inactivated by adding culture media.
All molecules demonstrated activity in trypsin inhibition.
Trypsin activity was stopped using culture medium.
It also contains the pancreatic enzymes trypsin.
Trypsin and chymotrypsin from bovine pancreas.
The concentration of trypsin at this time is not limited.
Trypsin is a digestive enzyme produced in the pancreas.
Amino groups released by a trypsin digestion control are subtracted.
The trypsin lysates were analyzed by electrophoresis as described above.
Thrombin is a member of the trypsin family of serine proteases.
Trypsin cleaves protein at arginine and lysine residues.
The sequences of these trypsin inhibitors are highly conserved.
Trypsin will be included as a positive control.
Various concentrations of trypsin and incubation times were tested.
Trypsin is added in order to obtain an optimum virus replication.
In some cases trypsin or bromelin are suitable.
Trypsin as digestion enzyme assuming max.
A serine proteinase such as trypsin or chymotrypsin is also preferred.
Trypsin and chymotrypsin are proteolytic enzymes.
Up to two missing cleavages of trypsin were allowed.
Inhibition of trypsin hydrolysis of haemoglobin is noncompetitive.
These bands are hydrolyzed using trypsin.
Neither chymotrypsin nor trypsin showed a significant effect.
Another imprinting molecule used is trypsin.
The trypsin inhibitor may be camostat.
No significant change in the activities of trypsin or chymotrypsin were detected.
When trypsin is used neutralization is achieved by other means.
Third solution comprising a proteolytic enzyme consisting in trypsin.
Chymotrypsin and trypsin are digestive enzymes.
And then digested with trypsin.
Trypsin neutralization solution was added and cells were collected.
Casein hydrolysed by pepsin and trypsin.
When trypsin is used neutralisation is achieved by other means.
The susceptibility of target epitopes to proteolysis by trypsin was determined.
