chymotrypsin


Also found in: Dictionary, Encyclopedia, Wikipedia.

chymotrypsin

 [ki″mo-trip´sin]
1. an enzyme with action similar to that of trypsin, produced in the intestine by activation of chymotrypsinogen.
2. a preparation crystallized from an extract of the pancreas of the ox, used clinically for enzymatic dissolution of the zonular membrane of the eye.

chy·mo·tryp·sin

(kī'mō-trip'sin),
Chymotrypsin A, B, or C; a serine proteinase of the gastrointestinal tract that preferentially cleaves carboxyl links of hydrophobic amino acids, particularly at tyrosyl, tryptophanyl, phenylalanyl, and leucyl residues; synthesized in the pancreas as chymotrypsinogen, and subsequently converted to π-, δ-, and finally α-chymotrypsin by successive trypsin-dependent cleavages; proposed for use in the treatment of inflammation and edema associated with trauma and to facilitate intracapsular cataract extraction; chymotrypsin A has the specificity described above, chymotrypsin B is homologous to chymotrypsin A, and chymotrypsin C has a broader specificity (for example, it acts additionally on carboxyl links of methionyl, glutaminyl, and asparaginyl residues).

chymotrypsin

(kī′mə-trĭp′sĭn)
n.
A pancreatic digestive enzyme that catalyzes the hydrolysis of certain proteins in the small intestine into polypeptides and amino acids.

chy′mo·tryp′tic (-tĭk) adj.

chymotrypsin

Physiology A GI tract serine protease synthesized in the pancreas as a prohormone, which cleaves proteins at hydrophobic amino acids–leucine, phenylalanine, tryptophan, tyrosine

chy·mo·tryp·sin

(kī'mō-trip'sin)
A serine proteinase of the gastrointestinal tract, synthesized in the pancreas as chymotrypsinogen; used in the treatment of inflammation and edema associated with trauma and to facilitate intracapsular cataract extraction.

chymotrypsin

An ENZYME that breaks down (digests) protein to amino acids and simpler substances. It is secreted by the pancreas and released into the DUODENUM. The enzyme is also used to clean wounds and in an earlier form of cataract surgery to cut the suspensory ligament (zonules) of the cataractous lens.

chymotrypsin

an enzyme found in the pancreatic juice of mammals that functions as an endopeptidase, catalysing the hydrolysis of PEPTIDE BONDS. It attacks the carboxyl groups of specific amino acids (phenylalanine, tyrosine, leucine, tryptophan, and methionine) and so produces large peptides. The enzyme works in the alkaline medium of the small intestine and is secreted by the pancreas in an inactive form.
References in periodicals archive ?
urophthalmus larvae diets indicates statistical differences for trypsin and chymotrypsin activities, where LO20 and LO25 presented the highest values (P < 0.05) (Table 4).
The hydrolysate of chymotrypsin showed 1374.0 and 176.20 J/g enthalpies corresponding to 88.518 and 123.550 0C denaturation temperatures respectively.
Hydrolysis by commercial trypsin and chymotrypsin and enzymes in midgut extracts from each strain was evaluated by spectrophotometry at 404 nm, using a test tube assay with 1% azocasein as substrate and 10 m incubation at room temperature, as described by Garcia-Carreno et al.
We found statistically significant correlations between increased resistance to itraconazole and higher enzymatic activity of naphthyl phosphohydrolase and alpha-galactosidase; increased resistance to fluconazole and higher enzymatic activity of trypsin and beta-glucosidase; increased susceptibility to 5-fluorocytosine and higher enzymatic activity of alkaline phosphatase, valine arylamidase, trypsin and chymotrypsin; increased susceptibility to ketoconazole and higher enzymatic activity of cystine arylamidase.
In penaeids, trypsin and chymotrypsin are the main proteinases, responsible for more than 60% of protein digestion (Galgani et al., 1984).
Szabo et al., "Comprehensive functional analysis of chymotrypsin C (CTRC) variants reveals distinct loss-of-function mechanisms associated with pancreatitis risk," Gut, vol.
In accordance with this evidence, our results showed that the biochar alone decreased cultivable microorganisms abundance, while it enhanced the activity of enzymes involved in phosphorus, nitrogen, and carbon cycling (alkaline phosphatase, acid phosphatase, phosphohydrolase, lipase-esterase, esterase, chymotrypsin, and trypsin).
A previous study reported that unheated EW contain protease inhibitors, which can inhibit the activity of trypsin, elastase and chymotrypsin [11].
Chymotrypsin cleaves peptide bond by aromatic residues, unlike trypsin that only cleaves peptide bond at lysine and arginine.