Chymotrypsin. Medical search

A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.

Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.

A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.

Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.

A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.

A genus of leguminous shrubs or trees, mainly tropical, yielding useful compounds such as ALKALOIDS and PLANT LECTINS.

Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.

Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.

Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.

A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.

A low-molecular-weight protein (minimum molecular weight 8000) which has the ability to inhibit trypsin as well as chymotrypsin at independent binding sites. It is characterized by a high cystine content and the absence of glycine.

A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

The sum of the weight of all the atoms in a molecule.

A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

The rate dynamics in chemical or physical systems.

A heterogeneous mixture of glycoproteins responsible for the gel structure of egg white. It has trypsin-inhibiting activity.

The inactive proenzyme of trypsin secreted by the pancreas, activated in the duodenum via cleavage by enteropeptidase. (Stedman, 25th ed)

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995)

Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.

Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.

Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.

Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

The process of cleaving a chemical compound by the addition of a molecule of water.

Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.

A high-molecular-weight protein (approximately 22,500) containing 198 amino acid residues. It is a strong inhibitor of trypsin and human plasmin.

Tests based on the biochemistry and physiology of the exocrine pancreas and involving analysis of blood, duodenal contents, feces, or urine for products of pancreatic secretion.

A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.

Glycoprotein found in alpha(1)-globulin region in human serum. It inhibits chymotrypsin-like proteinases in vivo and has cytotoxic killer-cell activity in vitro. The protein also has a role as an acute-phase protein and is active in the control of immunologic and inflammatory processes, and as a tumor marker. It is a member of the serpin superfamily.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

A group of amylolytic enzymes that cleave starch, glycogen, and related alpha-1,4-glucans. (Stedman, 25th ed) EC 3.2.1.-.

Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC 3.4.2.1 and EC 3.4.12.2.

A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-

Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.

Glycoproteins with a molecular weight of approximately 620,000 to 680,000. Precipitation by electrophoresis is in the alpha region. They include alpha 1-macroglobulins and alpha 2-macroglobulins. These proteins exhibit trypsin-, chymotrypsin-, thrombin-, and plasmin-binding activity and function as hormonal transporters.

A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

An actinomycete from which the antibiotics STREPTOMYCIN, grisein, and CANDICIDIN are obtained.

A malabsorption condition resulting from greater than 10% reduction in the secretion of pancreatic digestive enzymes (LIPASE; PROTEASES; and AMYLASE) by the EXOCRINE PANCREAS into the DUODENUM. This condition is often associated with CYSTIC FIBROSIS and with chronic PANCREATITIS.

A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. This family includes alpha 1-antitrypsin, angiotensinogen, ovalbumin, antiplasmin, alpha 1-antichymotrypsin, thyroxine-binding protein, complement 1 inactivators, antithrombin III, heparin cofactor II, plasminogen inactivators, gene Y protein, placental plasminogen activator inhibitor, and barley Z protein. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known.

The fluid containing digestive enzymes secreted by the pancreas in response to food in the duodenum.

An enzyme that catalyzes the hydrolysis of proteins, including elastin. It cleaves preferentially bonds at the carboxyl side of Ala and Val, with greater specificity for Ala. EC 3.4.21.37.

A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.

Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.

Fluids originating from the epithelial lining of the intestines, adjoining exocrine glands and from organs such as the liver, which empty into the cavity of the intestines.

A family of unenveloped RNA viruses with cubic symmetry. The twelve genera include ORTHOREOVIRUS; ORBIVIRUS; COLTIVIRUS; ROTAVIRUS; Aquareovirus, Cypovirus, Phytoreovirus, Fijivirus, Seadornavirus, Idnoreovirus, Mycoreovirus, and Oryzavirus.

The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.

The encapsulated embryos of flowering plants. They are used as is or for animal feed because of the high content of concentrated nutrients like starches, proteins, and fats. Rapeseed, cottonseed, and sunflower seed are also produced for the oils (fats) they yield.

Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.

Benzoic acid esters or salts substituted with one or more iodine atoms.

Proteins prepared by recombinant DNA technology.

Plants whose roots, leaves, seeds, bark, or other constituent parts possess therapeutic, tonic, purgative, curative or other pharmacologic attributes, when administered to man or animals.

A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction or the lysis of fibrin and quickly inactivated by antiplasmins.

Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.

A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.

The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.

Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

A proteolytic enzyme obtained from Streptomyces griseus.

Physiologically inactive substances that can be converted to active enzymes.

Electrophoresis in which paper is used as the diffusion medium. This technique is confined almost entirely to separations of small molecules such as amino acids, peptides, and nucleotides, and relatively high voltages are nearly always used.

A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.

R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low prolyl isomerase activity in both peptide and protein-folding assays. (1/2760)

Previously we reported that the R73A and H144Q variants of the yeast cyclophilin Cpr3 were virtually inactive in a protease-coupled peptide assay, but retained activity as catalysts of a proline-limited protein folding reaction [Scholz, C. et al. (1997) FEBS Lett. 414, 69-73]. A reinvestigation revealed that in fact these two mutations strongly decrease the prolyl isomerase activity of Cpr3 in both the peptide and the protein-folding assay. The high folding activities found previously originated from a contamination of the recombinant Cpr3 proteins with the Escherichia coli protein SlyD, a prolyl isomerase that co-purifies with His-tagged proteins. SlyD is inactive in the peptide assay, but highly active in the protein-folding assay. (+info)

Kinetic study of alpha-chymotrypsin catalysis with regard to the interaction between the specificity-determining site and the aromatic side chain of substrates. (2/2760)

In order to investigate how changes in the structures of side-chain aromatic groups of specific substrates influence binding and kinetic specificity in alpha chymotrypsin [EC 3.4.21.1]-catalyzed reactions, a number of nucleus-substituted derivatives of the specific ester substrates were prepared and steady-state kinetic studies were carried out at pH 6.5 and 7.8. Ac-Trp(NCps)-OMe was hydrolyzed more readily at low substrate concentration than Ac-Trp-OMe due to its smaller Km(app) value, suggesting that the bulky 2-nitro-4-carboxyphenylsulfenyl moiety interacts with outer residues rather than with those in the hydrophobic pocket and that this interaction increases the binding specificity. Inhibition experiments using the corresponding carboxylate and analogous inhibitors, however, showed that the carboxy group at the para position of the phenyl nucleus of the substituent sterically hinders association with the active site of alpha-chymotrypsin at pH 7.8 but not at pH 6.5. The kcat values of Ac-Trp(CHO)-0Me, Ac-Tyr(3-NO2)-OMe, and Ac-m-Tyr-OMe were much higher than those of the corresponding specific substrates, indicating that derivatives with a substitute as large as a formyl, nitro or hydroxyl group at the xi-position are stereochemically favorable to the catalytic process. Remarkable increases in Km(app) were also observed. The individual parameters for Ac-Dopa-OMe, however, were comparable to those for Ac-Tyr-OMe. (+info)

A method for analyzing enzyme kinetics with substrate activation and inhibition and its application to the alpha-chymotrypsin-catalyzed hydrolysis of phenyl acetates. (3/2760)

A general kinetic method was developed to analyze enzyme-catalyzed systems complicated by the presence of activation or inhibition by substrate. The method was applied to the alpha-chymotrypsin [EC 3.4.21.1]-catalyzed hydrolysis of p-chlorophenyl and p-methoxyphenyl acetates. Deacylation rate constants which were not complicated by substrate activation were obtained. The analysis shows that the abnormal substituent dependence of kcat in the steady state hydrolysis is due not to substrate activation but to inappropriateness of the two-step mechanism or the existence of more than one acetyl-enzyme intermediate. (+info)

The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptic and chymotryptic peptides and the complete sequence. (4/2760)

Peptic and chymotryptic peptides were isolated form the NADP-specific glutamate dehydrogenase of Neurospora crassa and substantially sequenced. Out of 452 residues in the polypeptide chain, 265 were recovered in the peptic and 427 in the chymotryptic peptides. Together with the tryptic peptides [Wootton, J. C., Taylor, J. G., Jackson, A. A., Chambers, G. K. & Fincham, J. R. S. (1975) Biochem. J. 149, 749-755], these establish the complete sequence of the chain, including the acid and amide assignments, except for seven places where overlaps are inadequate. These remaining alignments are deduced from information on the CNBr fragments obtained in another laboratory [Blumenthal, K. M., Moon, K. & Smith, E. L. (1975), J. Biol. Chem. 250, 3644-3654]. Further information has been deposited as Supplementary Publication SUP 50054 (17 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained under the terms given in Biochem. J. (1975) 145, 5. (+info)

Neuroregulation by vasoactive intestinal peptide (VIP) of mucus secretion in ferret trachea: activation of BK(Ca) channels and inhibition of neurotransmitter release. (5/2760)

1. The aims of this study were to determine: (1) whether vasoactive intestinal peptide (VIP) regulates cholinergic and 'sensory-efferent' (tachykininergic) 35SO4 labelled mucus output in ferret trachea in vitro, using a VIP antibody, (2) the class of potassium (K+) channel involved in VIP-regulation of cholinergic neural secretion using glibenclamide (an ATP-sensitive K+ (K(ATP)) channel inhibitor), iberiotoxin (a large conductance calcium activated K+ (BK(ca)) channel blocker), and apamin (a small conductance K(ca) (SK(ca)) channel blocker), and (3) the effect of VIP on cholinergic neurotransmission using [3H]-choline overflow as a marker for acetylcholine (ACh) release. 2. Exogenous VIP (1 and 10 microM) alone increased 35SO4 output by up to 53% above baseline, but suppressed (by up to 80% at 1 microM) cholinergic and tachykininergic neural secretion without altering secretion induced by ACh or substance P (1 microM each). Endogenous VIP accounted for the minor increase in non-adrenergic, non-cholinergic (NANC), non-tachykininergic neural secretion, which was compatible with the secretory response of exogenous VIP. 3. Iberiotoxin (3 microM), but not apamin (1 microM) or glibenclamide (0.1 microM), reversed the inhibition by VIP (10 nM) of cholinergic neural secretion. 4. Both endogenous VIP (by use of the VIP antibody; 1:500 dilution) and exogenous VIP (0.1 microM), the latter by 34%, inhibited ACh release from cholinergic nerve terminals and this suppression was completely reversed by iberiotoxin (0.1 microM). 5. We conclude that, in ferret trachea in vitro, endogenous VIP has dual activity whereby its small direct stimulatory action on mucus secretion is secondary to its marked regulation of cholinergic and tachykininergic neurogenic mucus secretion. Regulation is via inhibition of neurotransmitter release, consequent upon opening of BK(Ca) channels. In the context of neurogenic mucus secretion, we propose that VIP joins NO as a neurotransmitter of i-NANC nerves in ferret trachea. (+info)

Unexpected crucial role of residue 225 in serine proteases. (6/2760)

Residue 225 in serine proteases of the chymotrypsin family is Pro or Tyr in more than 95% of nearly 300 available sequences. Proteases with Y225 (like some blood coagulation and complement factors) are almost exclusively found in vertebrates, whereas proteases with P225 (like degradative enzymes) are present from bacteria to human. Saturation mutagenesis of Y225 in thrombin shows that residue 225 affects ligand recognition up to 60,000-fold. With the exception of Tyr and Phe, all residues are associated with comparable or greatly reduced catalytic activity relative to Pro. The crystal structures of three mutants that differ widely in catalytic activity (Y225F, Y225P, and Y225I) show that although residue 225 makes no contact with substrate, it drastically influences the shape of the water channel around the primary specificity site. The activity profiles obtained for thrombin also suggest that the conversion of Pro to Tyr or Phe documented in the vertebrates occurred through Ser and was driven by a significant gain (up to 50-fold) in catalytic activity. In fact, Ser and Phe are documented in 4% of serine proteases, which together with Pro and Tyr account for almost the entire distribution of residues at position 225. The unexpected crucial role of residue 225 in serine proteases explains the evolutionary selection of residues at this position and shows that the structural determinants of protease activity and specificity are more complex than currently believed. These findings have broad implications in the rational design of enzymes with enhanced catalytic properties. (+info)

Identification of protein-disulfide isomerase activity in fibronectin. (7/2760)

Assembly and degradation of fibronectin-containing extracellular matrices are dynamic processes that are up-regulated during wound healing, embryogenesis, and metastasis. Although several of the early steps leading to fibronectin deposition have been identified, the mechanisms leading to the accumulation of fibronectin in disulfide-stabilized multimers are largely unknown. Disulfide-stabilized fibronectin multimers are thought to arise through intra- or intermolecular disulfide exchange. Several proteins involved in disulfide exchange reactions contain the sequence Cys-X-X-Cys in their active sites, including thioredoxin and protein-disulfide isomerase. The twelfth type I module of fibronectin (I12) contains a Cys-X-X-Cys motif, suggesting that fibronectin may have the intrinsic ability to catalyze disulfide bond rearrangement. Using an established protein refolding assay, we demonstrate here that fibronectin has protein-disulfide isomerase activity and that this activity is localized to the carboxyl-terminal type I module I12. I12 was as active on an equal molar basis as intact fibronectin, indicating that most of the protein-disulfide isomerase activity of fibronectin is localized to I12. Moreover, the protein-disulfide isomerase activity of fibronectin appears to be partially cryptic since limited proteolysis of I10-I12 increased its isomerase activity and dramatically enhanced the rate of RNase refolding. This is the first demonstration that fibronectin contains protein-disulfide isomerase activity and suggests that cross-linking of fibronectin in the extracellular matrix may be catalyzed by a disulfide isomerase activity contained within the fibronectin molecule. (+info)

Isolation and identification of three bactericidal domains in the bovine alpha-lactalbumin molecule. (8/2760)

Proteolytic digestion of alpha-lactalbumin by pepsin, trypsin and chymotrypsin yielded three polypeptide fragments with bactericidal properties. Two fragments were obtained from the tryptic digestion. One was a pentapeptide with the sequence EQLTK (residues 1-5) and the other, GYGGVSLPEWVCTTF ALCSEK (residues (17-31)S-S(109-114)), was composed of two polypeptide chains held together by a disulfide bridge. Fragmentation of alpha-lactalbumin by chymotrypsin yielded CKDDQNPH ISCDKF (residues (61-68)S-S(75-80)), also a polypeptide composed of two polypeptide chains held together by a disulfide bridge. The three polypeptides were synthesized and found to exert antimicrobial activities. The polypeptides were mostly active against Gram-positive bacteria. Gram-negative bacteria were only poorly susceptible to the bactericidal action of the polypeptides. GYGGVSLPEWVCTTF ALCSEK was most, EQLTK least bactericidal. Replacement of leucine (23) with isoleucine, having a similar chemical structure but higher hydrophobicity, in the sequence GYGGVSLPEWVCTTF ALCSEK significantly reduced the bactericidal capacity of the polypeptide. Digestion of alpha-lactalbumin by pepsin yielded several polypeptide fragments without antibacterial activity. alpha-Lactalbumin in contrast to its polypeptide fragments was not bactericidal against all the bacterial strains tested. Our results suggest a possible antimicrobial function of alpha-lactalbumin after its partial digestion by endopeptidases. (+info)

... (EC 3.4.21.1, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, ... Wilcox PE (1970). "[5] Chymotrypsinogens-chymotrypsins". Chymotrypsinogens - chymotrypsins. Methods in Enzymology. Vol. 19. pp ... producing α-chymotrypsin (which is more active and stable than π-chymotrypsin). The resulting molecule is a three-polypeptide ... alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the ...

https://en.wikipedia.org/wiki/Chymotrypsin

Chymotrypsin C, also known as caldecrin or elastase 4, is an enzyme that in humans is encoded by the CTRC gene. Chymotrypsin C ... Brecher AS, Yang MP (1998). "Acetaldehyde inhibits chymotrypsin and serum anti-chymotrypsin activity". J. Investig. Med. 46 (4 ... "Entrez Gene: chymotrypsin C (caldecrin)". Tomomura A, Akiyama M, Itoh H, Yoshino I, Tomomura M, Nishii Y, Noikura T, Saheki T ( ... 2008). "Chymotrypsin C (CTRC) alterations that diminish activity or secretion are associated with chronic pancreatitis". Nat. ...

https://en.wikipedia.org/wiki/Chymotrypsin-C

Chymotrypsin+C at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.21). ... Chymotrypsin C (EC 3.4.21.2) is an enzyme. This enzyme catalyses the following chemical reaction: Preferential cleavage: Leu-, ... Folk, J.E. (1970). "Chymotrypsin C (porcine pancreas)". Methods Enzymol. Methods in Enzymology. 19: 109-112. doi:10.1016/0076- ... Wilcox PE (1970). "Chymotrypsinogens - chymotrypsins". Methods Enzymol. Methods in Enzymology. 19: 64-108. doi:10.1016/0076- ...

https://en.wikipedia.org/wiki/Chymotrypsin_C

More generally, he made a study of mechanisms for chymotrypsin catalysis., and in particular the "charge-relay" system as a way ... Bruice, T. C. (1961). "The Mechanisms for Chymotrypsin". Proceedings of the National Academy of Sciences. 47 (12): 1924-1928. ...

https://en.wikipedia.org/wiki/Thomas_Bruice

Discoveries of polyester degrading enzymes date at least as far back as 1975 (α-chymotrypsin) and 1977 (lipase) for example. ... Tabushi I, Yamada H, Matsuzaki H, Furukawa J (August 1975). "Polyester readily hydrolyzable by chymotrypsin". Journal of ...

https://en.wikipedia.org/wiki/PETase

Chymotrypsin-like protease CTRL-1 is an enzyme that in humans is encoded by the CTRL gene. GRCh38: Ensembl release 89: ... "Entrez Gene: CTRL chymotrypsin-like". Human CTRL genome location and CTRL gene details page in the UCSC Genome Browser. ... Heidtmann HH, Travis J (1994). "A novel chymotrypsin-like serine proteinase from human lung". Biol. Chem. Hoppe-Seyler. 374 (9 ... 1997). "A novel human chymotrypsin-like digestive enzyme". J. Biol. Chem. 272 (12): 8099-104. doi:10.1074/jbc.272.12.8099. PMID ...

https://en.wikipedia.org/wiki/CTRL_(gene)

Chymotrypsin-like elastase family member 2B is and enzyme that in humans is encoded by the CELA2B gene. Elastases form a ... "Entrez Gene: chymotrypsin-like elastase family". Human CELA2B genome location and CELA2B gene details page in the UCSC Genome ...

https://en.wikipedia.org/wiki/CELA2B

Early in his career, Knowles studied α-chymotrypsin and pepsin, which are nonspecific proteases, meaning they accept a broad ... Ingles, DW; Knowles, JR (1967). "Specificity and stereospecificity of α-chymotrypsin". Biochemical Journal. 104 (2): 369-377. ...

https://en.wikipedia.org/wiki/Jeremy_R._Knowles

Trypsin- and chymotrypsin-inhibitor from soybeans". International Journal of Peptide and Protein Research. 25 (2): 113-31. doi: ...

https://en.wikipedia.org/wiki/Bowman–Birk_protease_inhibitor

Gutfreund, H.; Sturtevant, J. M. (1956). "The Mechanism of Chymotrypsin-Catalyzed Reactions". Proceedings of the National ... including chymotrypsin and trypsin, and was especially active in using methods of studying fast reactions to study enzyme ...

https://en.wikipedia.org/wiki/Herbert_Gutfreund

1. Chymotrypsin Catalyzed Hydrolysis of p-Nitroanilides of Phenylalanine and Tyrosine Attached to Side-Chains of Copolymers of ... 6. Hydrophilic Gels Cleavable by Chymotrypsin". Biomaterials 3, 150-154 (1982) J. Kopeček, P. Rejmanová, V. Chytrý, "Polymers ...

https://en.wikipedia.org/wiki/Jindřich_Kopeček

Hartley, BS; V Massey (1956). "The active center of chymotrypsin: 1. Labelling with a fluorescent dye". Biochimica et ...

https://en.wikipedia.org/wiki/Dansyl_chloride

It inhibits proteases like chymotrypsin, kallikrein, plasmin, thrombin, and trypsin. The specificity is similar to the ... Formation and Reactions of Phenylmethanesulfonyl α-Chymotrypsin". Biochemistry. 3 (6): 783-791. doi:10.1021/bi00894a009. PMID ...

https://en.wikipedia.org/wiki/AEBSF

Chymotrypsin, trypsin and Diclofenac are also recommended. "Osteoarthritis". The Lecturio Medical Concept Library. Retrieved 27 ...

https://en.wikipedia.org/wiki/Knee_effusion

Bernal JD, Fankuchen I, Perutz M (1938). "X-ray study of chymotrypsin and hemoglobin". Nature. 141: 523-524. doi:10.1038/ ... The early crystal structures included chymotrypsin (PDB file 2CHA), chymotrypsinogen (PDB file 1CHG), trypsin (PDB file 1PTN), ... Matthews BW, Sigler PB, Henderson R, Blow DM (1967). "Three-dimensional structure of tosyl-α-chymotrypsin". Nature. 214 (5089 ... comparison with α-chymotrypsin, and implications for zymogen activation". Biochemistry. 9 (9): 1997-2009. doi:10.1021/ ...

https://en.wikipedia.org/wiki/List_of_biophysically_important_macromolecular_crystal_structures

TPCK is an irreversible inhibitor of chymotrypsin. Also inhibits some cysteine proteases such as caspase, papain, bromelain or ... as in chymotrypsin, in which it binds to the Histidine-57 residue in the active site). TPCK-treated trypsin is used to improve ...

https://en.wikipedia.org/wiki/Tosyl_phenylalanyl_chloromethyl_ketone

Fersht AR, Sperling J (February 1973). "The charge relay system in chymotrypsin and chymotrypsinogen". J. Mol. Biol. 74 (2): ...

https://en.wikipedia.org/wiki/Histone_methyltransferase

Postoperative ocular hypertension from use of alpha chymotrypsin. Glaucoma of miscellaneous origin Associated with intraocular ... Drug-induced glaucoma Corticosteroid induced glaucoma Alpha-chymotrypsin glaucoma. ...

https://en.wikipedia.org/wiki/Glaucoma

Some SSI's also inhibit trypsin, chymotrypsin and griselysin. Commercially, SSI's have huge potential in the commercial market ...

https://en.wikipedia.org/wiki/SSI_protease_inhibitor

Chymotrypsin-like elastase family member 3B also known as elastase-3B, protease E, or fecal elastase is an enzyme that in ... September 2004). "Fecal chymotrypsin and elastase-1 determination on one single stool collected at random: diagnostic value for ... chymotrypsin and kallikrein, it has a digestive function in the intestine. Elastase 3B preferentially cleaves proteins after ... literature that describes human elastase 1 activity in the pancreas or fecal material is actually referring to chymotrypsin- ...

https://en.wikipedia.org/wiki/CELA3B

They inhibit chymotrypsin, a peptidase belong to the S1 family (INTERPRO). Rawlings ND, Tolle DP, Barrett AJ (2004). " ... Pacifastin inhibits the serine peptidases trypsin and chymotrypsin. All pacifastin members that have been characterized at the ...

https://en.wikipedia.org/wiki/Pacifastin

Bernal, J. D.; Fankuchen, I.; Perutz, MAX (1938). "An X-Ray Study of Chymotrypsin and Haemoglobin". Nature. 141 (3568): 523-524 ... Bernal during which time they examined the structure of chymotrypsin and haemoglobin. He also collaborated with Bernal's ...

https://en.wikipedia.org/wiki/Isidor_Fankuchen

Bender, Myron L.; Zerner, Burt (1961). "The formation of the acyl-enzyme intermediate, trans-cinnamoyl-α-chymotrypsin, in the ... Kezdy, Ferenc J.; Bender, Myron L. (1962). "The Kinetics of the α-Chymotrypsin-Catalyzed Hydrolysis of p-Nitrophenyl Acetate". ... Brot, Frederick E.; Bender, Myron L. (1969). "Use of the specificity constant of α-chymotrypsin". Journal of the American ... Bender, Myron L.; Kezdy, Ferenc J. (1964). "The Current Status of the α-Chymotrypsin Mechanism". Journal of the American ...

https://en.wikipedia.org/wiki/Myron_L._Bender

In chymotrypsin, these residues are Ser-195, His-57 and Asp-102. The mechanism of chymotrypsin can be divided into two phases. ... 137-9 Chymotrypsin is a serine endopeptidase that is present in pancreatic juice and helps the hydrolysis of proteins and ... Jansen EF, Nuttig F, Balls AK (1949). "Mode of inhibition of chymotrypsin by diisopropyl fluorophosphate; introduction of ...

https://en.wikipedia.org/wiki/Active_site

The enzymes trypsin and chymotrypsin were first purified in the 1930s. A serine in each of trypsin and chymotrypsin was ... The structure of chymotrypsin was solved by X-ray crystallography in the 1960s, showing the orientation of the catalytic triad ... Blow DM, Birktoft JJ, Hartley BS (1969). "Role of a buried acid group in the mechanism of action of chymotrypsin". Nature. 221 ... The triad is exemplified by chymotrypsin, a model serine protease from the PA superfamily which uses its triad to hydrolyse ...

https://en.wikipedia.org/wiki/Catalytic_triad

Genetically engineered mutants of the chymotrypsin serine protease were shown to have some proteinase activity even though ... McLachlan AD (February 1979). "Gene duplications in the structural evolution of chymotrypsin". Journal of Molecular Biology. ...

https://en.wikipedia.org/wiki/Protein_domain

This mechanism is utilised by the catalytic triad of enzymes such as proteases like chymotrypsin and trypsin, where an acyl- ... For example, the energetics of the covalent bond to the serine molecule in chymotrypsin should be compared to the well- ... Fersht AR, Requena Y (December 1971). "Mechanism of the -chymotrypsin-catalyzed hydrolysis of amides. pH dependence of k c and ... Consider the reaction of peptide bond hydrolysis catalyzed by a pure protein α-chymotrypsin (an enzyme acting without a ...

https://en.wikipedia.org/wiki/Enzyme_catalysis

Additionally, trypsin inhibitor partially interferes with chymotrypsin function. Trypsinogen is an inactive form of trypsin, ... is formed in the pancreas and activated to trypsin with enteropeptidase Chymotrypsinogen is the inactive form of chymotrypsin ...

https://en.wikipedia.org/wiki/Trypsin_inhibitor

Purification and properties, and formation of pi-chymotrypsin". The Biochemical Journal. 147 (1): 45-53. doi:10.1042/bj1470045 ...

https://en.wikipedia.org/wiki/Aspergillopepsin_I

Stevenson KJ, Gibson D, Dixon GH (February 1974). "Amino acid analyses of chymotrypsin-like proteases from the sea anemone ( ... Gibson D, Dixon GH (May 1969). "Chymotrypsin-like proteases from the sea anemone, Metridium senile". Nature. 222 (5195): 753-6 ...

https://en.wikipedia.org/wiki/Metridin

Chymotrypsin is an enzyme released by the pancreas during digestion. If the amount is lower than normal, it may mean your ... This test measures the amount of chymotrypsin in a stool sample. ... Other names: fecal chymotrypsin, trypsin and chymotrypsin stool ... What is a chymotrypsin in stool test?. This test measures the amount of chymotrypsin in a stool sample. Chymotrypsin is an ... Why do I need a chymotrypsin in stool test?. You may need this test if you have symptoms of a pancreatic disorder. These ...

https://medlineplus.gov/lab-tests/chymotrypsin-in-stool/

When the pancreas does not produce enough trypsin and chymotrypsin. ... Trypsin and chymotrypsin are substances released from the pancreas during normal digestion. ... If trypsin or chymotrypsin are present, the gelatin will clear.. How to Prepare for the Test. Your provider will provide you ... Stool - trypsin and chymotrypsin. How the Test is Performed. There are many ways to collect the samples. Your health care ...

https://www.ucsfhealth.org/medical-tests/trypsin-and-chymotrypsin-in-stool

Learn more about Chymotrypsin health benefits, uses, side effects, effectiveness, safety, precautions, and warnings ... A-Chymotrypsin, A-Chymotrypsine, Alpha-Chymotrypsin, Alpha-Chymotrypsine, Chymotrypsin A, Chymotrypsine A, Chymotrypsin B, ... People use chymotrypsin to make medicine.. People take chymotrypsin by mouth or as a shot to reduce redness and swelling ... Chymotrypsin is safe when used in the eye by a healthcare professional. Chymotrypsin can cause side effects when used in the ...

https://www.rxlist.com/chymotrypsin/supplements.htm

The stool chymotrypsin concentrations increased from birth to a maximum at 4 days of age and then fell again over the next four ... Measuring faecal chymotrypsin concentrations is a reliable procedure for identifying pancreatic exocrine insufficiency in the ... In eight babies, also with suspected meconium ileus but with negative sweat tests, chymotrypsin concentrations were within the ... faecal chymotrypsin concentrations were all appreciably reduced. ... Faecal chymotrypsin concentrations in neonates with cystic ...

https://adc.bmj.com/content/63/10/1229

Chymotrypsin in the IUPHAR/BPS Guide to PHARMACOLOGY. ... chymotrypsin C Show summary »« Hide summary More detailed page ... chymotrypsin like elastase 1 Previous and unofficial names. chymotrypsin-like elastase family , chymotrypsin like elastase ... chymotrypsin C Previous and unofficial names. CLCR , ELA4 , elastase 4 , serum calcium-decreasing factor , chymotrypsin C ( ... S1: Chymotrypsin C. Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for ...

https://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=751

π Hydrogen Bond between Dipeptide Side Chains as a Structural Essential for Chymotrypsin Inhibition. In Peptide Chemistry 1995 ... π Hydrogen Bond between Dipeptide Side Chains as a Structural Essential for Chymotrypsin Inhibition. / Maeda, Iori; ... π Hydrogen Bond between Dipeptide Side Chains as a Structural Essential for Chymotrypsin Inhibition. Peptide Chemistry 1995. ... title = "π Hydrogen Bond between Dipeptide Side Chains as a Structural Essential for Chymotrypsin Inhibition", ...

https://kyushu-u.pure.elsevier.com/en/publications/%CF%80-hydrogen-bond-between-dipeptide-side-chains-as-a-structural-ess

A Molecular Dynamics Study of the Stability of Chymotrypsin Acyl Enzymes. Guy W. Bemis, Gail Carlson-Golab, John A. ... Bemis, G. W., Carlson-Golab, G., & Katzenellenbogen, J. A. (1992). A Molecular Dynamics Study of the Stability of Chymotrypsin ... A Molecular Dynamics Study of the Stability of Chymotrypsin Acyl Enzymes. Journal of the American Chemical Society. 1992 Jan 1; ... Bemis, Guy W. ; Carlson-Golab, Gail ; Katzenellenbogen, John A. / A Molecular Dynamics Study of the Stability of Chymotrypsin ...

https://experts.illinois.edu/en/publications/a-molecular-dynamics-study-of-the-stability-of-chymotrypsin-acyl-

5.6.2. Chymotrypsin. Chymotrypsin inhibition assays were performed as described [38], with following modifications: the pH of ... Inhibitory activity against chymotrypsin and thrombin was potent in some of the fractions but the activity increased with ... Louis, MO, USA). Chymotrypsin (Sigma-Aldrich, St. Louis, MO, USA) from bovine pancreas was used. Six concentrations (60, 100, ... Sano, T.; Kaya, K. Oscillamide Y, a chymotrypsin inhibitor from toxic Oscillatoria agardhii. Tetrahedron Lett. 1995, 36, 5933- ...

https://www.mdpi.com/2072-6651/8/4/108

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A colorimetric method for the estimation of the esterolytic activity of chymotrypsin. Indian Journal of Biochemistry & ... A colorimetric method for the estimation of the esterolytic activity of chymotrypsin. ...

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We find that chymotrypsin loses part of its helical content upon adsorption, with minor perturbation of its overall tertiary ... Atomistic Details of Chymotrypsin Conformational Changes upon Adsorption on Silica. Hildebrand, Nils;Michaelis, Monika;Wurzler ... We find that chymotrypsin loses part of its helical content upon adsorption, with minor perturbation of its overall tertiary ... Atomistic Details of Chymotrypsin Conformational Changes upon Adsorption on Silica / Hildebrand, Nils; Michaelis, Monika; ...

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Sensitive to trypsin, chymotrypsin and papain (34) Virion Morphology. Shape. Dimensions. 18-26 nm ...

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DcCoV, dromedary camel coronavirus; 3CLpro, chymotrypsin-like protease; RdRp, RNA-dependent RNA polymerase; S protein, spike ...

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Trypsin Chymotrypsin EnzymeTrypsin Chymotrypsin Enzyme belongs to the class of serine proteases and catalyze used for the ... Trypsin Chymotrypsin Enzyme By ENZYME BIOSCIENCE PVT. LTD.ENZYME BIOSCIENCE PVT. LTD.. ...

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found in: IPTG, 4-Methylumbelliferyl phosphate, bis(2-amino-2-methyl-1,3-propanediol) salt, alpha-Chymotrypsin, MUG, BCIP/NBT ...

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Occurrence as well as the subcellular activities of trypsin and chymotrypsin have been demonstrated in the developing human ... Occurrence and subcellular activities of trypsin and chymotrypsin in the developing human placenta. S MISRA, J KUSHARI, M ... Occurrence as well as the subcellular activities of trypsin and chymotrypsin have been demonstrated in the developing human ...

https://research.caluniv.ac.in/publication/occurrence-and-subcellular-activities-of-trypsin-and-chymotrypsin

Potential applicability of chymotrypsin-susceptible microcin J25 derivatives to food preservation. María Fernanda Pomares, Raúl ... Potential applicability of chymotrypsin-susceptible microcin J25 derivatives to food preservation. В: Applied and Environmental ... Potential applicability of chymotrypsin-susceptible microcin J25 derivatives to food preservation. Applied and Environmental ... In the present paper, we describe a chymotrypsin-susceptible MccJ25 derivative with a mutation of Gly12 to Tyr that retained ...

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... treated with 0.01 mg/ml Chymotrypsin. d. Full size representation of the immunoblots on Chymotrypsinized and Trypsinized ...

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Transgenic indica rice cultivar Swarna expressing a potato chymotrypsin inhibitor pin2 gene show enhanced levels of ... expressing a potato chymotrypsin inhibitor pin2 gene show enhanced levels of resistance to yellow stem borer Plant Cell, Tissue ... with a potato chymotrypsin inhibitor gene (pin2) through Agrobacterium-mediated transformation. Four out of nine primary ...

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It has been demonstrated that selective inhibition of the chymotrypsin-like (CT-L) activity of constitutive-(c20S) and immuno-( ... It has been demonstrated that selective inhibition of the chymotrypsin-like (CT-L) activity of constitutive-(c20S) and immuno-( ... It has been demonstrated that selective inhibition of the chymotrypsin-like (CT-L) activity of constitutive-(c20S) and immuno-( ... It has been demonstrated that selective inhibition of the chymotrypsin-like (CT-L) activity of constitutive-(c20S) and immuno-( ...

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... A series of beta-lactam derivatives has been designed and synthesized to inhibit the chymotrypsin-like activity of the human ... potent and selective inhibitors of the chymotrypsin-like activity of the human 20S proteasome. Bioorganic & Medicinal Chemistry ...

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... the pancreatic digestive enzymes trypsin and chymotrypsin; and their inactive precursors trypsinogen and chymotrypsinogen. ...

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Three-dimensional structure of tosyl-alpha-chymotrypsin. Matthews BW, Sigler PB, Henderson R, Blow DM. Matthews BW, et al. ...

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Trypsin and chymotrypsin are substances released from the pancreas during normal digestion. (ucsfhealth.org)
When the pancreas does not produce enough trypsin and chymotrypsin, smaller-than-normal amounts can be seen in a stool sample. (ucsfhealth.org)
This article discusses the test to measure trypsin and chymotrypsin in stool. (ucsfhealth.org)

Chymotrypsin is an enzyme released by the pancreas during digestion. (medlineplus.gov)
Your sample may also be tested for trypsin, an enzyme released by the pancreas along with chymotrypsin. (medlineplus.gov)
Chymotrypsin is an enzyme. (rxlist.com)
We have investigated the enantioselectivity observed in the deacylation rates of a β-substituted β-phenylpropionyl chymotrypsin acyl enzyme by molecular dynamics simulations. (illinois.edu)
Trypsin Chymotrypsin Tablet is a prescription-strength oral proteolytic enzyme preparation that has been in clinical use since the 1960s. (schwitzbiotech.co.in)
Trypsin Chymotrypsin Enzyme By Enzyme Bioscience Pvt. (tradeindia.com)
Thus, the enzyme constitutes the first known natural variation of the chymotrypsin-like triad in which a carboxylic acid is replaced by a neutral hydrogen-bond acceptor. (rcsb.org)
Chymotrypsin-targeting FLISP probes interact with active catalytic sites of chymotrypsin-like proteases, so cells with greater quantities of active chymotrypsin-like enzyme activity with a greater fluorescence potential than those that are not upregulated. (immunochemistry.com)
If there is an active chymotrypsin-like enzyme inside the cell, it will covalently bind with the FLISP inhibitor, in this case SR101-Leu-CMK (SLCK), and retain the red fluorescent signal inside the cell. (immunochemistry.com)
Cells containing lower concentrations of chymotrypsin-like enzyme activity will retain a lower level of fluorescence compared to cells containing higher concentrations of this effector enzyme component. (immunochemistry.com)

PSA is a chymotrypsin-like serine protease (kallikrein family) exclusively produced by the prostate epithelium, and abundant in seminal fluid. (novusbio.com)
Quantitate intracellular chymotrypsin-like serine protease activity in vitro with ICT's FLISP kits. (immunochemistry.com)
The relative thermoresistance of GRAM and the sensitivity of GRAM against treatment with protease or chymotrypsin suggested a protein nature of GRAM. (cdc.gov)
Inhibits SARS-CoV-2 chymotrypsin-like protease (3CLpro). (mayflowerbio.com)

If the amount of chymotrypsin and/or trypsin is below normal, it may mean your pancreas isn't making enough enzymes to digest your food properly. (medlineplus.gov)
Structures for both R and S acyl enzymes were constructed starting from the X-ray structure of chymotrypsin phenylethaneboronic acid complex. (illinois.edu)
Bemis, GW, Carlson-Golab, G & Katzenellenbogen, JA 1992, ' A Molecular Dynamics Study of the Stability of Chymotrypsin Acyl Enzymes ', Journal of the American Chemical Society , vol. 114, no. 2, pp. 570-578. (illinois.edu)
Alpha-chymotrypsin (ChTRP), also stored as alpha-chymotrypsinogen (ChTRPz), represents the principal trypsin contaminant since both enzymes exhibit chemical similarities. (conicet.gov.ar)

Three-dimensional structure of tosyl-alpha-chymotrypsin. (nih.gov)
Entrapment of alpha-chymotrypsin into hollow polyelectrolyte microcapsules. (mpg.de)

In the present work the covalent structure has been determined and its homologous relationship to those of chymotrypsin, trypsin, and elastase has been established (approximately 33% identity with each). (northwestern.edu)
Three disulfide bonds in GSP occur in similar positions in chymotrypsin, trypsin, and elastase. (northwestern.edu)

Rao, G. J. N. (2009) Transgenic indica rice cultivar 'Swarna' expressing a potato chymotrypsin inhibitor pin2 gene show enhanced levels of resistance to yellow stem borer Plant Cell, Tissue and Organ Culture, 99 (3). (ias.ac.in)
Transgenic rice was developed from 'Swarna', the most popular indica rice cultivar (Oryza sativa L.) in South East Asia, with a potato chymotrypsin inhibitor gene (pin2) through Agrobacterium-mediated transformation. (ias.ac.in)
ICID_SOLTU Wound-induced proteinase inhibitor I precursor (Chymotrypsin inhibitor I, D subunit) g. (cornell.edu)

Measuring faecal chymotrypsin concentrations is a reliable procedure for identifying pancreatic exocrine insufficiency in the newborn. (bmj.com)

We demonstrate that the C-terminal helical fragment is unfolded as an isolated oligopeptide in pure water, folded as an α-helix as terminus of chymotrypsin in solution, and again partly disordered when the protein is adsorbed on silica. (sissa.it)

However, GSP lacks a disulfide bond which is present in all known serine proteases (linking Cys-191 to Cys-220 in chymotrypsin). (northwestern.edu)

What is a chymotrypsin in stool test? (medlineplus.gov)
This test measures the amount of chymotrypsin in a stool sample. (medlineplus.gov)
Why do I need a chymotrypsin in stool test? (medlineplus.gov)
You don't need any special preparations for a chymotrypsin in stool test. (medlineplus.gov)
Your results will show whether the amount of chymotrypsin in your stool is normal or below normal. (medlineplus.gov)
The result is normal if there is a normal amount of trypsin or chymotrypsin in the stool. (ucsfhealth.org)
An abnormal result means the trypsin or chymotrypsin levels in your stool are below the normal range. (ucsfhealth.org)
The stool chymotrypsin concentrations increased from birth to a maximum at 4 days of age and then fell again over the next four days. (bmj.com)

It has been demonstrated that selective inhibition of the chymotrypsin-like (CT-L) activity of constitutive-(c20S) and immuno-(i20S) proteasome represents a valid strategy to induce antineoplastic effect in hematologic tumors. (elsevier.com)

Comprehensive screening of chymotrypsin C (CTRC) gene in tropical calcific pancreatitis identifies novel variants. (cdc.gov)

Faecal chymotrypsin concentrations in neonates with cystic fibrosis and healthy controls. (bmj.com)
In a second group of 22 newborn babies suspected of meconium ileus and later confirmed to have cystic fibrosis, faecal chymotrypsin concentrations were all appreciably reduced. (bmj.com)
In eight babies, also with suspected meconium ileus but with negative sweat tests, chymotrypsin concentrations were within the healthy newborn range. (bmj.com)

Latha B, Ramakrishnan M, Jayaraman V, Babu M. Serum enzymatic changes modulated using trypsin: chymotrypsin preparation during burn wounds in humans. (rxlist.com)

To reduce tissue damage in burn patients: a 6:1 ratio (trypsin:chymotrypsin), in a combined amount of 200,000 units USP four times daily for ten days. (rxlist.com)

IMSEAR at SEARO: A colorimetric method for the estimation of the esterolytic activity of chymotrypsin. (who.int)
In the present paper, we describe a chymotrypsin-susceptible MccJ25 derivative with a mutation of Gly 12 to Tyr that retained almost full antibiotic activity and efficiently inhibited the growth of pathogenic Salmonella enterica serovar Newport and Escherichia coli O157:H7 in skim milk and egg yolk. (skoltech.ru)
Novel beta-lactam derivatives: potent and selective inhibitors of the chymotrypsin-like activity of the human 20S proteasome. (novartis.com)
A series of beta-lactam derivatives has been designed and synthesized to inhibit the chymotrypsin-like activity of the human 20S proteasome. (novartis.com)

We find that chymotrypsin loses part of its helical content upon adsorption, with minor perturbation of its overall tertiary structure, associated with changes in the aromatic interactions. (sissa.it)

Healthcare providers inject a solution of chymotrypsin into the eyes as part of cataract surgery. (rxlist.com)

Latha B, Ramakrishnan M, Jayaraman V, Babu M. The efficacy of trypsin: chymotrypsin preparation in the reduction of oxidative damage during burn injury. (rxlist.com)

More evidence is needed to rate the effectiveness of chymotrypsin for these uses. (rxlist.com)

Chymotrypsin is sometimes breathed in (inhaled) or applied to the skin (used topically) for conditions that involve pain and swelling (inflammation) and for infections. (rxlist.com)
Chymotrypsin can cause side effects when used in the eye, including an increase in pressure in the eye and other eye conditions such as uveitis, paralysis of the iris, and keratitis. (rxlist.com)

If the amount of chymotrypsin and/or trypsin is below normal, it may mean your pancreas isn't making enough enzymes to digest your food properly. (medlineplus.gov)
This test checks your stool sample for trypsin and chymotrypsin, two enzymes made by the pancreas. (baycare.org)
Evidence of pancreatic enzymes trypsin and chymotrypsin. (aaan.org)
Protien digestion is carried out by several enzymes such as pepsin, trypsin, enterokinase and chymotrypsin. (topperlearning.com)
You may also wish to take proteolytic enzymes such as chymotrypsin and trypsin, which break down amino acids, and have been shown to speed up healing in sports injuries. (healthy.net)
The proteolytic enzymes trypsin and chymotrypsin partially digest proteins. (farmpally.com)

Medizym contains the scientifically studied combination of bromelain papin, pancreatin, trypsin, chymotrypsin and rutin. (naturally.com)
Chymotrypsin is usually a pork product, so vegetarians and other persons who do not eat pork may prefer bromelain or papain. (healthifybody.com)

The serpins (SERine Proteinase INhibitors) are a family of proteins with important physiological roles, including but not limited to the inhibition of chymotrypsin-like serine proteinases. (elsevier.com)

Abnormal levels of trypsin or chymotrypsin mean that your pancreas isn't working properly. (baycare.org)
Both chymotrypsin and amylase are produced by the pancreas and play important roles in digestion. (nih.gov)
Abnormal levels of chymotrypsin and amylase have been known to occur with multiple pancreas-related disorders, including pancreatitis. (nih.gov)
Chymotrypsin is naturally produced by the pancreas in the human body. (innerzyme.com)
Chymotrypsinogen -- The inactive proenzyme secreted by the pancreas that is subsequently converted to chymotrypsin. (nih.gov)

Effects of polyhydroxy compounds on the structure and activity of alpha-chymotrypsin , BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 293: pp. 416-420. (doktori.hu)
Structure and activity of alpha-chymotrypsin and trypsin in aqueous organic media , BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 280: pp. 1367-1371. (doktori.hu)

Chymotrypsin, trypsin, or trypsin/chymotrypsin was used to digest cervid PrP, resulting in a set of 18 peptides spanning the 20 polymorphic sites. (usda.gov)

Trypsin breaks down proteins into peptide chains and Chymotrypsin breaks down peptide chains into amino acids. (wereyouwondering.com)
This IMCD preparation was split into 3 samples, and the proteins digested with either trypsin (1 microg trypsin: 20 microg sample, digested overnight 25C), chymotrypsin (1 microg chymotrypsin: 40 microg sample, digested overnight 25C) or ASP-n (1 microg ASP-N: 100 microg sample, digested overnight 37C). (nih.gov)
In digestion, trypsin, chymotrypsin and elastase work together to chop up proteins. (rcsb.org)

The 20S regular proteasome offers three main proteolytic actions described as caspase-, trypsin- and chymotrypsin-like, with the related catalytic sites becoming designated to the subunits 1, Rabbit Polyclonal to ABHD12B 2 and 5, [20] respectively. (cancerhugs.com)

Recently, chymotrypsin C (CTRC) variants that diminish its activity or secretion were found to predict susceptibility to chronic pancreatitis (CP). (nih.gov)

no trypsin chymotrypsin with diclofenac potassium tablets Grade 4 events and 1 death (Grade 5) was reported. (praudyogiki.in)

The α -Chymotrypsin-catalyzed Hydrolysis of Acetyl-, Chloroacetyl- and Benzoyl-L-valine Methyl Eater. (go.jp)
Chymotrypsin also catalyses the hydrolysis of ester bonds. (nih.gov)
Hydrolysis rates of lysobactin at pH 7.5 with active or inactivated chymotrypsin were measured and were compared with the rate of chymotrypsin hydrolysis of the open-chain form following hydrolysis of the lactone. (aspetjournals.org)

The ability to inhibit trypsin is higher than that of chymotrypsin and plasmin. (everychina.net)

Our results demonstrate that the tumor proteasome β5 subunit is the primary target of WA, and inhibition of the proteasomal chymotrypsin-like activity by WA in vivo is responsible for, or contributes to, the antitumor effect of this ancient medicinal compound. (aspetjournals.org)
Shows only marginal inhibition of the chymotrypsin-like activity of the proteasome. (enzolifesciences.com)

Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. (abcam.com)

I recently carried out an investigation into the specificity of chymotrypsin and trypsin which I am in the process of writing up. (webqc.org)

The primary uses of chymotrypsin are as a naturally anti-inflammatory and as a digestive aid. (innerzyme.com)
As a natural anti-inflammatory, chymotrypsin may help reduce tissue damage and the formation of fibrin clots during inflammation. (innerzyme.com)

Under the urgent need to restore morality and ethics, otherwise America before the civil war (trypsin chymotrypsin with diclofenac potassium). (praudyogiki.in)
Deze regeling is aanzienlijk goedkoper dan rechtstreeks aan BUMA betalen en scheelt veel ( diclofenac potassium nombre generico ) administratieve rompslomp. (praudyogiki.in)

This test measures the amount of chymotrypsin in a stool sample. (medlineplus.gov)

4. Chymotrypsin as well as trypsin could activate the inactive renin although less effectively. (portlandpress.com)
the isoelectric points of the native, the trypsin-activated and the chymotrypsin-activated forms of renin occurred at pH 5.3, 5.1 and 4.8 respectively. (portlandpress.com)

The invention relates to rabbit antisera raised against purified human chymotrypsin and amylase. (nih.gov)

N-benzoyl-DL-arginine-p-nitroanilide (BAPNA) and N-succinyl-L-phenylalanine-p-nitroanilide (NSPLN) were the synthetic substrates used to be recognised by trypsin and chymotrypsin, respectively. (webqc.org)

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R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low prolyl isomerase activity in both peptide and protein-folding assays. (1/2760)

Kinetic study of alpha-chymotrypsin catalysis with regard to the interaction between the specificity-determining site and the aromatic side chain of substrates. (2/2760)

A method for analyzing enzyme kinetics with substrate activation and inhibition and its application to the alpha-chymotrypsin-catalyzed hydrolysis of phenyl acetates. (3/2760)

The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptic and chymotryptic peptides and the complete sequence. (4/2760)

Neuroregulation by vasoactive intestinal peptide (VIP) of mucus secretion in ferret trachea: activation of BK(Ca) channels and inhibition of neurotransmitter release. (5/2760)

Unexpected crucial role of residue 225 in serine proteases. (6/2760)

Identification of protein-disulfide isomerase activity in fibronectin. (7/2760)

Isolation and identification of three bactericidal domains in the bovine alpha-lactalbumin molecule. (8/2760)

Chymotrypsin

Trypsin Inhibitors

Trypsin

Serine Proteinase Inhibitors

Pancreatic Elastase

Erythrina

Protease Inhibitors

Amino Acid Sequence

Chymotrypsinogen

Peptide Hydrolases

Serine Endopeptidases

Peptide Fragments

Pancreas

Trypsin Inhibitor, Bowman-Birk Soybean

Endopeptidases

Molecular Sequence Data

Molecular Weight

Cathepsin G

Binding Sites

Kinetics

Ovomucin

Trypsinogen

Electrophoresis, Polyacrylamide Gel

Protein Conformation

Aprotinin

Amino Acids

Cyanogen Bromide

Carboxypeptidases

Plant Proteins

Peptides

Cattle

Hydrolysis

Pepsin A

Trypsin Inhibitor, Kunitz Soybean

Pancreatic Function Tests

Thermolysin

alpha 1-Antichymotrypsin

Substrate Specificity

Hydrogen-Ion Concentration

Amylases

Carboxypeptidases A

Subtilisins

Chromatography, Gel

alpha-Macroglobulins

Cathepsins

Models, Molecular

Protein Binding

Streptomyces griseus

Exocrine Pancreatic Insufficiency

Serpins

Pancreatic Juice

Leukocyte Elastase

Papain

alpha 1-Antitrypsin

Intestinal Secretions

Reoviridae

Structure-Activity Relationship

Seeds

Chromatography, High Pressure Liquid

Iodobenzoates

Recombinant Proteins

Plants, Medicinal

Fibrinolysin

Peptide Mapping

Chemistry

Chemical Phenomena

Macromolecular Substances

Sequence Homology, Amino Acid

Pronase

Enzyme Precursors

Electrophoresis, Paper

Chromatography, Affinity

Chromatography, Ion Exchange

R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low prolyl isomerase activity in both peptide and protein-folding assays. (1/2760)

Kinetic study of alpha-chymotrypsin catalysis with regard to the interaction between the specificity-determining site and the aromatic side chain of substrates. (2/2760)

A method for analyzing enzyme kinetics with substrate activation and inhibition and its application to the alpha-chymotrypsin-catalyzed hydrolysis of phenyl acetates. (3/2760)

The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptic and chymotryptic peptides and the complete sequence. (4/2760)

Neuroregulation by vasoactive intestinal peptide (VIP) of mucus secretion in ferret trachea: activation of BK(Ca) channels and inhibition of neurotransmitter release. (5/2760)

Unexpected crucial role of residue 225 in serine proteases. (6/2760)

Identification of protein-disulfide isomerase activity in fibronectin. (7/2760)

$Gentaur Molecular :Kamiya \ Human Alpha 1 Anti Chymotrypsin ELISA \ KT-498$ Gentaur Molecular :Kamiya \ Human Alpha 1 Anti Chymotrypsin ELISA \ KT-498