trypsin Antonyms
No Synonyms and anytonyms found
Meaning of trypsin
trypsin (n)
an enzyme of pancreatic origin; catalyzes the hydrolysis of proteins to smaller polypeptide units
trypsin (n.)
A proteolytic ferment, or enzyme, present in the pancreatic juice. Unlike the pepsin of the gastric juice, it acts in a neutral or alkaline fluid, and not only converts the albuminous matter of the food into soluble peptones, but also, in part, into leucin and tyrosin.
trypsin Sentence Examples
- Trypsin, a digestive enzyme, plays a crucial role in breaking down proteins in the small intestine.
- Trypsin is synthesized in the pancreas as an inactive precursor called trypsinogen.
- The conversion of trypsinogen to active trypsin requires the presence of the enzyme enterokinase.
- Trypsin is responsible for cleaving specific peptide bonds on the carboxyl side of lysine and arginine residues.
- Trypsin is essential for the digestion of dietary proteins into smaller peptides and amino acids.
- Dysregulation of trypsin activity can lead to digestive disorders such as pancreatitis.
- Trypsin inhibitors are naturally occurring proteins that regulate trypsin activity in the body.
- Trypsin is used in various industrial applications, including the production of leather and pharmaceuticals.
- Researchers are exploring the use of trypsin in the development of new therapeutic approaches for cancer and other diseases.
- Trypsin-based assays are widely employed in biochemistry and molecular biology for protein characterization and analysis.
FAQs About the word trypsin
an enzyme of pancreatic origin; catalyzes the hydrolysis of proteins to smaller polypeptide unitsA proteolytic ferment, or enzyme, present in the pancreatic jui
No synonyms found.
No antonyms found.
Trypsin, a digestive enzyme, plays a crucial role in breaking down proteins in the small intestine.
Trypsin is synthesized in the pancreas as an inactive precursor called trypsinogen.
The conversion of trypsinogen to active trypsin requires the presence of the enzyme enterokinase.
Trypsin is responsible for cleaving specific peptide bonds on the carboxyl side of lysine and arginine residues.
