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Topic: Chymotrypsin


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In the News (Sun 21 Jul 19)

  
  Chymotrypsin - Wikipedia, the free encyclopedia
Chymotrypsin is synthesized in the pancreas by protein biosynthesis as a precursor called chymotrypsinogen that is enzymatically inactive.
The main substrates of chymotrypsin include tryptophan, tyrosine, phenylalanine, and methionine, which are cleaved at the carboxyl terminal.
Chymotrypsin cleaves peptide bonds by attacking the unreactive carbonyl group with a powerful nucleophile, the serine 195 residue located in the active site of the enzyme, which briefly becomes covalently bonded to the substrate, forming an enzyme-substrate intermediate.
en.wikipedia.org /wiki/Chymotrypsin   (354 words)

  
 InterPro: IPR001314 Peptidase S1A, chymotrypsin
Chymotrypsin, subtilisin and carboxypeptidase C clans have a catalytic triad of serine, aspartate and histidine in common: serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base [ 1 ].
Members of the chymotrypsin family may occasionally function intracellularly (for example, the intracellular digestion of bacteria in neutrophils), but most function extracellularly, for example in roles such as food digestion, fibrinolysis and complement activation [ 1 ].
The essential catalytic unit of the chymotrypsin family is around 220 amino acids in length, although the protein may be extended at the N-terminus with unrelated sequences, often containing modules.
www.ebi.ac.uk /interpro/IEntry?ac=IPR001314   (3098 words)

  
 Gale Encyclopedia of Alternative Medicine: Chymotrypsin
Chymotrypsin is a digestive enzyme that breaks down proteins (i.e., it is a proteolytic enzyme; it can also be referred to as a protease).
Chymotrypsin, as a hydrolase type of enzyme (which means it adds a water molecule during the breakdown process) acts by catalyzing the hydrolysis of peptide bonds of proteins in the small intestine.
Chymotrypsin, along with the other pancreatic enzymes, is most often used in the treatment of pancreatic insufficiency.
www.findarticles.com /p/articles/mi_g2603/is_0002/ai_2603000281   (961 words)

  
 89B-3 Purification and biochemical characterization of chymotrypsin from the viscera of Monterey sardine (Sardinops ...
Purification and biochemical characterization of chymotrypsin from the viscera of Monterey sardine (Sardinops sagax caerulea)
In this study, we present data on purification and the main biochemical characteristics of chymotrypsin from Monterey sardine viscera with the aim to contribute with alternatives for the commercial use of this by-product.
Chymotrypsin was isolated from the viscera of Monterey sardine by ammonium sulphate fractionation, gel filtration and ionic exchange chromatography, and then it was characterized on its main biochemical features.
ift.confex.com /ift/2005/techprogram/paper_31232.htm   (401 words)

  
 CHYMOTRYPSIN
Chymotrypsin hydrolyzes the peptide bond of amino acids with large hydrophobic side chains, such as phenylalanine, tryptophan, and tyrosine.
Chymotrypsin consists of 3 chains, A (Blue), B (Aqua), and C (Green).
The three separate chains of the activated chymotrypsin are formed when two dipeptide units, consisting of residues 14 and 15 and residues 147 and 148 are removed.
www.bio.davidson.edu /Courses/Molbio/MolStudents/spring2003/MaloneyH/chymotrypsinbuttons.html   (321 words)

  
 Princeton Separations Products Endopeptidase Modified Chymotrypsin Bovine   (Site not responding. Last check: 2007-10-12)
Princeton Separations Sequencing grade, Modified Chymotrypsin is first treated with TPCK and then subjected to an extensive purification process to remove contaminating protease and chymotryptic autolysis by-products, which could affect the specificity of the digestion process.
Thus the Princeton Separations Modified Chymotrypsin retains in excess of 80% of its activity after six hours at 30°C in reaction buffer, and in excess of 70% of its activity under the same conditions after 24 hours.
The Modified Chymotrypsin activity is monitored by assays developed in house which relate to its activity in sequencing applications.
www.prinsep.com /html/products/endopeptidases/chymotrypsin   (393 words)

  
 [No title]   (Site not responding. Last check: 2007-10-12)
determining a quantitative level of chymotrypsin present in the sample, and correlating the quantitative level of chymotrypsin determined to be present in the sample with the PDD to determine the efficacy of treating the individual individual secretin, secretin, neuropeptides, neuropeptides, or digestive enzyme administration.
It is postulated that the abnormal levels of chymotrypsin are due to the inability of the pancreas to release bicarbonate ions, due to the lack of secretin mechanization in the small intestines.
The method of claim 9, wherein the at least one threshold chymotrypsin level is based on a level of chymotrypsin associated with at least one other individual of the same approximate age that does not have the disorder.
www.wipo.int /cgi-pct/guest/getbykey5?KEY=01/43764.010621&ELEMENT_SET=DECL   (5190 words)

  
 Worthington Chymotrypsin
Chymotrypsin preferentially catalyzes the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine and tryptophan.
Chymotrypsin catalyzes the hydrolysis of bonds of leucyl, methionyl, asparaginyl and glutamyl residues.
An activity of 45 units per mg using the above definition, is the equivalent of 10,000 optical density or 1330 N.F. units per mg using ATEE as a substrate.
www.worthington-biochem.com /CHY/cat.html   (194 words)

  
 Untitled Document   (Site not responding. Last check: 2007-10-12)
chymotrypsin is a proteolytic enzyme that digests proteins in the small intestine.
Chymotrypsin is classified as a serine protease because there is a serine at the active site of the enzyme that directly participates in the breaking of the peptide bond.
The active site of chymotrypsin contains the side chains of aspartate 102 (aspartate 102 is the 102 nd amino acid from the N-terminal end of chymotrypsin), the side chain of histidine-57 and the side chain of serine-195.
academic.brooklyn.cuny.edu /biology/bio4fv/page/fr758271.htm   (112 words)

  
 Chymotrypsin
Although an enzyme called pepsin begins to digest protein molecules while they are in our stomach, most of the digestion of protein takes place after the food leaves the stomach and moves into the small intestines.
For example, chymotrypsin’s one enzymatic function is to accelerate the breaking of peptide bonds that link an amino acid that has a nonpolar side chain, like phenylalanine, to another amino acid on the interior of polypeptide chains.
The shape, size, and amino acid sequence of chymotrypsin’s active site allow that part of the enzyme to bind a portion of a polypeptide that has nonpolar side chains, like those found in phenylalanine.
www.mpcfaculty.net /mark_bishop/chymotrypsin.htm   (741 words)

  
 AllRefer.com - chymotrypsin (Biochemistry) - Encyclopedia
Chymotrypsin is produced in the pancreas as the inactive, or zymogen, form chymotrypsinogen.
Along with other digestive enzymes of the pancreas, chymotrypsinogen is carried in the pancreatic juice through the pancreatic duct into the duodenum.
Partly because it was one of the first enzymes available commercially in crystalline form, chymotrypsin has been studied extensively.
reference.allrefer.com /encyclopedia/C/chymotry.html   (194 words)

  
 ARS | Publication request: Alpha-Chymotrypsin Catalysis in Imidazolium-Based Ionic Liquids   (Site not responding. Last check: 2007-10-12)
Chymotrypsin, an enzyme that normally cleaves proteins but under special conditions can perform valuable synthetic reactions, was tested in ionic liquids and shown to be synthetically active.
Chymotrypsin was studied to determine whether trends in solvent polarity and water activity, and enzyme support properties, observed with this enzyme in conventional organic solvents hold for the novel environment provided by ionic liquids.
Chymotrypsin freeze-dried with K2HPO4, KCl, or poly(ethylene glycol) demonstrated no activity in [bmim][PF6] or [omim][PF6] at very low water concentrations, but moderate transesterification rates were observed with the ionic liquids containing 0.25 % water (v/v) and higher.
www.ars.usda.gov /research/publications/publications.htm?SEQ_NO_115=118129   (341 words)

  
 Biophysical Journal: Specificity of Trypsin and Chymotrypsin: Loop-Motion-Controlled Dynamic Correlation as a ...   (Site not responding. Last check: 2007-10-12)
We have found that trypsin and chymotrypsin have distinct dynamic signatures in the two loop regions, which are in turn highly correlated with motions of certain residues in the binding pockets.
Interestingly, replacing the two loops of trypsin with those of chymotrypsin changes the motion style of trypsin to chymotrypsin-like, whereas the same experimental replacement was shown necessary to make trypsin have chymotrypsin's enzyme specificity and activity.
When the two loops L1 and L2 of trypsin were replaced by those of chymotrypsin in addition to the D189S mutation, the new protein shows an increase of chymotrypsin activity to ~1000-fold against the D189S mutant (1).
www.findarticles.com /p/articles/mi_qa3938/is_200508/ai_n14898948   (1429 words)

  
 MedlinePlus Medical Encyclopedia: Trypsin and chymotrypsin in stool
If trypsin or chymotrypsin are present, the gelatin will be digested, which will produce a clearing of the gelatin.
Trypsin and chymotrypsin are proteolytic enzymes released from the pancreas during normal digestion.
A normal result is normal concentration of trypsin or chymotrypsin in the stool.
www.nlm.nih.gov /medlineplus/ency/article/003594.htm   (538 words)

  
 The differential specificity of chymotrypsin A and B is determined by amino acid 226 -- Hudáky et al. 259 (1): ...   (Site not responding. Last check: 2007-10-12)
The differential specificity of chymotrypsin A and B is determined by amino acid 226 -- Hudáky et al.
The differential specificity of chymotrypsin A and B is determined by amino acid 226
The A and B isoforms of the pancreatic serine proteinase, chymotrypsin
content.febsjournal.org /cgi/content/abstract/259/1/528   (325 words)

  
 catalysis   (Site not responding. Last check: 2007-10-12)
Chymotrypsin is classified as a serine protease because there is a serine in the active site of the enzyme.
The 57th amino acid of the primary sequence of chymotrypsin is Histidine (His57), the 102nd amino acid is aspartic acid (asp102) and the 195th amino acid is serine (ser 195).
In an animation of catalysis carried out by chymotrypsin, the red lines and arrows indicate the series of covalent bonds that are borken or formed in the process of breaking one peptide bond
academic.brooklyn.cuny.edu /biology/bio4fv/page/catalysp.htm   (199 words)

  
 Worthington Chymotrypsin
Fastrez, J., and Fersht, A.: Demonstration of the Acyl-Enzyme Mechanism for the Hydrolysis of Peptides and Anilides by Chymotrypsin, Biochem 12, 2025, 1973
Gutfreund, H., and Sturtevant, J.: The Mechanism of the Reaction of Chymotrypsin with p-Nitrophenyl Acetate, Biochem J 63, 656, 1956
Kullmann, W.: Kinetics of Chymotrypsin- and Papain-catalyzed Synthesis of [Leucine]enkephalin and [Methionine]enkephalin, Biochem J 220, 405, 1984
www.worthington-biochem.com /CHY   (6410 words)

  
 Biophysical Journal: Single-Molecule Enzymology of Chymotrypsin Using Water-in-Oil Emulsion
The assay utilizes a synthetic chymotrypsin substrate that is nonfluorescent before cleavage by chymotrypsin, but is intensely fluorescent afterward.
We obtained chymotrypsin from Sigma Chemical, where it is purified from bovine pancreas.
The single-molecule chymotrypsin assay is performed by loading the emulsion into a grid-like polydimethylsiloxane microfluidic device (Whitesides et al., 2001) bonded to a glass coverslip, which provides a chamber with a dimension of 200 × 200 × 35 µm.
www.findarticles.com /p/articles/mi_qa3938/is_200506/ai_n13642563   (1350 words)

  
 Enzeco® Trypsin/Chymotrypsin 1:1
Both Trypsin, 3.4.21.4, and Chymotrypsin 3.4.21.1, are classed as serine Proteases.
The Chymotrypsin activity is approximately 1000 Units/ milligram.
A unit of activity is defined as the amount of enzyme causing a decrease in absorbance at 237 nm of 0.0075 per minute at 25 degrees Celsius.
www.foodingredientsonline.com /Content/ProductShowcase/product.asp?DocID={C2111EAC-1FAE-11D5-A770-00D0B7694F32}&VNETCOOKIE=NO   (157 words)

  
 InterPro: IPR001254 Peptidase S1 and S6, chymotrypsin/Hap   (Site not responding. Last check: 2007-10-12)
This group of serine proteases belong to the MEROPS peptidase family S1 (chymotrypsin family, clan PA(S))and to peptidase family S6 (Hap serine peptidases).
The chymotrypsin family is almost totally confined to animals, although trypsin-like enzymes are found in actinomycetes of the genera Streptomyces and Saccharopolyspora, and in the fungus Fusarium oxysporum [ 1 ].
The enzymes are inherently secreted, being synthesised with a signal peptide that targets them to the secretory pathway.
www.ebi.ac.uk /interpro/IEntry?ac=IPR001254   (3152 words)

  
 Three Chymotrypsin Genes Are Members of the AdpA Regulon in the A-Factor Regulatory Cascade in Streptomyces griseus -- ...   (Site not responding. Last check: 2007-10-12)
Three Chymotrypsin Genes Are Members of the AdpA Regulon in the A-Factor Regulatory Cascade in Streptomyces griseus -- Tomono et al.
Deletion of the chromosomal spr genes and chymotrypsin activities of the mutants.
Chymotrypsin activities were measured as described for panel B. wt, wild type.
jb.asm.org /cgi/content/full/187/18/6341   (7093 words)

  
 Proteolytic Enzymes
Papain and bromelain are the respective names for the proteolytic enzymes found in these fruits.
The enzymes made in your body are called trypsin and chymotrypsin.
For use as a supplement, trypsin and chymotrypsin are extracted from the pancreas of various animals.
healthlibrary.epnet.com /GetContent.aspx?token=e0498803-7f62-4563-8d47-5fe33da65dd4&chunkiid=21671   (2317 words)

  
 Specificity of Trypsin and Chymotrypsin: Loop Motion Controlled Dynamic Correlation as a Determinant -- Ma et al., ...
Articles by Ma, W. Articles by Lai, L. Specificity of Trypsin and Chymotrypsin: Loop Motion Controlled Dynamic Correlation as a Determinant
Trypsin and chymotrypsin are both serine proteases with high
chymotrypsin and the roles played by the two loops.
www.biophysj.org /cgi/content/abstract/biophysj.104.057158v1   (230 words)

  
 AllRefer Health - Trypsin and Chymotrypsin in Stool: How is the Test Performed? (Stool - Trypsin and Chymotrypsin)
AllRefer Health - Trypsin and Chymotrypsin in Stool: How is the Test Performed?
You are here : AllRefer.com > Health > Tests and Exams > Trypsin and Chymotrypsin in Stool: How is the Test Performed?
Main Page of Trypsin and Chymotrypsin in Stool
health.allrefer.com /health/trypsin-and-chymotrypsin-in-stool-perform.html   (392 words)

  
 Medical Encyclopedia: Trypsin and chymotrypsin in stool (Print Version)
Medical Encyclopedia: Trypsin and chymotrypsin in stool (Print Version)
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www.nlm.nih.gov /medlineplus/print/ency/article/003594.htm   (489 words)

  
 Specificity of Trypsin and Chymotrypsin: Loop-Motion-Controlled Dynamic Correlation as a Determinant -- Ma et al. 89 ...
Specificity of Trypsin and Chymotrypsin: Loop-Motion-Controlled Dynamic Correlation as a Determinant -- Ma et al.
trypsin and chymotrypsin and the roles played by the two loops.
of trypsin with those of chymotrypsin changes the motion style
www.biophysj.org /cgi/content/abstract/89/2/1183   (254 words)

  
 Chymotrypsin Discontinuation   (Site not responding. Last check: 2007-10-12)
There is no other CHYMOTRYPSIN ophthalmic product available
Chymotrypsin is indicated for zonulysis prior to intracapsular lens extraction.
No other ophthalmic product has this indication, so there is no therapeutic substitution that can be recommended for this agent.
depts.washington.edu /druginfo/Alerts/Details/chymo.html   (55 words)

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