How do you use Chymotrypsin in a sentence? See 6 example sentences showing how this word appears in different contexts, plus the exact meaning.
Chymotrypsin meaning
An endopeptidase enzyme that cleaves peptides at the carboxyl side of tyrosine, tryptophan, and phenylalanine amino acids.
Using Chymotrypsin
- The main meaning on this page is: An endopeptidase enzyme that cleaves peptides at the carboxyl side of tyrosine, tryptophan, and phenylalanine amino acids.
Context around Chymotrypsin
- Average sentence length in these examples: 22 words
- Position in the sentence: 2 start, 2 middle, 2 end
- Sentence types: 6 statements, 0 questions, 0 exclamations
Corpus analysis for Chymotrypsin
- In this selection, "chymotrypsin" usually appears near the start of the sentence. The average example has 22 words, and this corpus slice is mostly made up of statements.
- Around the word, activation, proteases, enable and explains stand out and add context to how "chymotrypsin" is used.
- Recognizable usage signals include action of chymotrypsin explains this and activation chymotrypsin is synthesized. That gives this page its own corpus information beyond isolated example sentences.
- By corpus frequency, "chymotrypsin" sits close to words such as aaas, aacc and aacs, which helps place it inside the broader word index.
Example types with chymotrypsin
The same corpus examples are grouped by length and sentence type, making it easier to see the contexts in which the word appears:
The mode of action of chymotrypsin explains this as hydrolysis takes place in two steps. (15 words)
Trypsin activates chymotrypsinogen by cleaving peptidic bonds in positions Arg15 - Ile16 and produces π-Chymotrypsin. (15 words)
Activation Chymotrypsin is synthesized in the pancreas by protein biosynthesis as a precursor called chymotrypsinogen that is enzymatically inactive. (19 words)
Like many proteases, chymotrypsin will also hydrolyse amide bonds in vitro, a virtue that enabled the use of substrate analogs such as N-acetyl-L-phenylalanine p-nitrophenyl amide for enzyme assays. (32 words)
Acid proteases secreted into the stomach (such as pepsin ) and serine proteases present in duodenum ( trypsin and chymotrypsin ) enable us to digest the protein in food. (26 words)
The trypsin, once activated, can also cleave other trypsinogens as well as the precursors of other proteases such as chymotrypsin and carboxypeptidase to activate them. (25 words)
Example sentences (6)
Acid proteases secreted into the stomach (such as pepsin ) and serine proteases present in duodenum ( trypsin and chymotrypsin ) enable us to digest the protein in food.
Activation Chymotrypsin is synthesized in the pancreas by protein biosynthesis as a precursor called chymotrypsinogen that is enzymatically inactive.
Like many proteases, chymotrypsin will also hydrolyse amide bonds in vitro, a virtue that enabled the use of substrate analogs such as N-acetyl-L-phenylalanine p-nitrophenyl amide for enzyme assays.
The mode of action of chymotrypsin explains this as hydrolysis takes place in two steps.
The trypsin, once activated, can also cleave other trypsinogens as well as the precursors of other proteases such as chymotrypsin and carboxypeptidase to activate them.
Trypsin activates chymotrypsinogen by cleaving peptidic bonds in positions Arg15 - Ile16 and produces π-Chymotrypsin.