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trypsin::noun | Spocien Dictionary
| Type | Words |
|---|---|
| Type of | enzyme |
| Has types | trypsinogen |
Examples of trypsin
trypsin
Normal cooking processes degrade lectins and trypsin inhibitors to harmless forms.
From the en.wikipedia.org
The mixture was then diluted 4-fold to 2 M urea and digested overnight with trypsin.
From the nature.com
Ovorubin can bind itself to trypsin, a common digestive enzyme that breaks down proteins.
From the newscientist.com
Pancreatitis occurs when the enzyme trypsin dissolves cells from within.
From the sciencedaily.com
Trypsin is a digestive enzyme used in biological research and pharmaceutical processing.
From the infowars.com
G-banding is obtained with Giemsa stain following digestion of chromosomes with trypsin.
From the en.wikipedia.org
Discard both unused, thawed trypsin and digestion solution after use.
From the nature.com
At 10,000 pounds-per-square-inch up to 35,000 psi, trypsin appeared to maximally cleave albumin.
From the sciencedaily.com
The following days, cells were harvested by trypsin treatment and counted with a haemocytometer.
From the nature.com
- An enzyme of pancreatic origin; catalyzes the hydrolysis of proteins to smaller polypeptide units
- 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. ...
- An enzyme that is produced by the pancreas. It is a protease.
- An important pancreatic enzyme which breaks down proteins.
- A proteolytic enzyme that hydrolyzes peptide bonds on the carboxyl side of the amino acids arginine and lysine.
- A protein digesting enzyme made by the pancreas and active in the small intestine.
- A serine protease that cuts preferentially on the carboxylate side of basic amino acid residues in a polypeptide.
- An enzyme capable of cleaving peptide bonds. It is used to remove adherent cells from a surface and to break up (digest) purified proteins for analysis.
