chymotrypsin

(redirected from Chymotripsin)
Also found in: Dictionary, Encyclopedia.

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.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

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).
Farlex Partner Medical Dictionary © Farlex 2012

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.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.

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
McGraw-Hill Concise Dictionary of Modern Medicine. © 2002 by The McGraw-Hill Companies, Inc.

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.
Medical Dictionary for the Health Professions and Nursing © Farlex 2012

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.
Collins Dictionary of Medicine © Robert M. Youngson 2004, 2005

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.
Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005