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> Chemicals & Drugs > Amino Acid > Chymotrypsin

Chymotrypsin

Chymotrypsin: A serine protease enzyme that plays a key role in the digestion of proteins.
It catalyzes the hydrolysis of peptide bonds, preferentially cleaving on the carboxy side of aromatic amino acids like tyrosine, tryptophan, and phenyalanine.
Chymotrypsin is produced in the pancreas and secreted into the duodenum, where it helps break down dietary proteins into smaller peptides and amino acids for absorption.
Its activitiy is regulated by other pancreatic enzymes and can be inhibited by certain compounds.
Understanding chymotrypsin's structure, function, and regulation is crucial for research on digestive processes and related disorders.

Most cited protocols related to «Chymotrypsin»

1
Evaluating Peptide Identification Algorithms
Cited 40 times
We used four previously described data sets to test our algorithms [17 (link)]. The first is a yeast data set containing 69,705 target PSMs and twice that number of decoy PSMs. These data were acquired from a tryptic digest of an unfractionated yeast lysate and analyzed using a four-hour reverse phase separation. Throughout this work, peptide were assigned to spectra by using SEQUEST with no enzyme specificity and with no amino acid modifications enabled. The next two data sets were derived from the same yeast lysate, but treated by different proteolytic enzymes: elastase and chymotrypsin. These data sets respectively contain 57,860 and 60,217 target PSMs and twice that number of decoy PSMs. The final data set was derived from a C. elegans lysate proteolytically digested by trypsin and processed analogously to the yeast data sets.
Each PSM was represented using the 17 features listed in Table 1. Note that, originally, Percolator used 20 features. In this work, we removed three features that exploit protein-level information, because of the difficulty of accurately validating, via decoy database search, methods that use this type of information. We also defined 20 additional features for each peptide, also defined in Table 1, corresponding to the counts of amino acids in the given peptide. Using these addition features yields a feature vector of length 37.
Spivak M., Weston J., Bottou L., Käll L, & Noble W.S. (2009). Improvements to the Percolator algorithm for peptide identification from shotgun proteomics data sets. Journal of proteome research, 8(7), 3737-3745.
Publication 2009
Amino Acids Chymotrypsin Cloning Vectors Enzymes Pancreatic Elastase Peptide Hydrolases Peptides Proteins Saccharomyces cerevisiae Trypsin
2
SARS-CoV-2 Spike Protein Analysis
Cited 14 times
Dithiothreitol (DTT) and iodoacetamide (IAA) were purchased from Sigma Aldrich (St. Louis, MO). Sequencing-grade modified trypsin and chymotrypsin were purchased from Promega (Madison, WI). All other reagents were purchased from Sigma Aldrich unless indicated otherwise. Data analysis was performed using Byonic 3.5 software and manually using Xcalibur 4.2. The SARS-CoV-2 spike protein culture supernatant subunit S1 (Cat. No. 230-20407) and subunit S2 (Cat. No. 230-20408), and purified subunit S2 (Cat. No. 230-30163) were purchased from RayBiotech (Atlanta, GA).
Shajahan A., Supekar N.T., Gleinich A.S, & Azadi P. (2020). Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2. Glycobiology, 30(12), 981-988.
Publication 2020
Chymotrypsin Dithiothreitol Iodoacetamide Promega Protein Subunits spike protein, SARS-CoV-2 Trypsin
3
Synthesis and Purification of Surfactant Peptides
Cited 12 times
MB (34 amino acid sequence: NH2-CWLCRALIKRIQAMIPKGGRMLPQLVCRLVLRCSCOOH; see Fig. 2B), S-MB (41 amino acid sequence: NH2-FPIPLPYCWLCRALIKRIQAMIPKGGRMLPQLVCRLVLRCS-COOH; see Fig. 2A) and SP-B(1–8) [8 amino acid sequence: NH2-FPIPLPYC-CONH2] were prepared with either a ABI 431A solid phase peptide synthesizer (Applied Biosystems, Foster City, CA) configured for FastMoc™ chemistry [54] (link), a Symphony Multiple Peptide Synthesizer (Protein Technologies, Tucson, AZ) using standard Fmoc synthesis, or a Liberty Microwave Peptide Synthesizer (CEM Corp., Matthews, NC) configured for standard Fmoc synthesis. A low substitution (0.3 mmole/gm) pre-derivatized Fmoc-serine (tBu) Wang resin (NovaBiochem, San Diego, CA) or H-Ser(OtBu)-HMPB Nova PEG resin (NovaBiochem, San Diego, CA) were used to minimize the formation of truncated sequences with the MB and S-MB peptide, while a Rink Amide MBHA resin (NovaBiochem, San Diego, CA) was employed for synthesis of the SP-B(1–8) peptide. All residues were double-coupled to insure optimal yield [48] (link). After synthesis of the respective linear sequences, peptides were cleaved from the resin and deprotected using a mixture of 0.75 gm phenol, 0.25 ml ethanedithiol, 0.5 ml of thioanisole, 0.5 ml of deionized water and 10 ml trifluoroacetic acid per gram of resin initially chilled to 5°C, and then allowed to come to 25°C with continuous stirring over a period of 2 h to insure complete peptide deprotection [48] (link). Crude peptides were removed from the resin by vacuum-assisted filtration, and by washing on a medium porosity sintered glass filter with trifluoroacetic acid and dichloromethane to maximize yield. Filtered crude peptides were precipitated in ice cold tertiary butyl ether, and separated by centrifugation at 2000×g for 10 min (2–3 cycles of ether-precipitation and centrifugation were used to minimize cleavage-deprotection byproducts). Reduced crude peptides from ether-precipitation were verified for molecular mass by MALDI-TOF spectroscopy, dissolved in trifluoroethanol (TFE):10 mM HCl (1∶1, v∶v), freeze dried, and purified by preparative HPLC [48] (link). Final folding of HPLC-purified peptides was facilitated by air-oxidation for at least 48 h at 25°C in TFE and 10 mM ammonium bicarbonate buffer (4∶6, v∶v) at pH 8.0 [55] (link). Final oxidized MB and S-MB were re-purified by reverse phase HPLC, verified in molecular mass via MALDI-TOF, and disulfide connectivity was confirmed by mass spectroscopy of enzyme-digested fragments (trypsin and chymotrypsin digestion).
Walther F.J., Waring A.J., Hernandez-Juviel J.M., Gordon L.M., Wang Z., Jung C.L., Ruchala P., Clark A.P., Smith W.M., Sharma S, & Notter R.H. (2010). Critical Structural and Functional Roles for the N-Terminal Insertion Sequence in Surfactant Protein B Analogs. PLoS ONE, 5(1), e8672.
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Publication 2010
Amino Acid Sequence ammonium bicarbonate Anabolism Buffers Centrifugation Chymotrypsin Cold Temperature Cytokinesis Digestion Disulfides Enzymes ethanedithiol Ethers Ethers, Cyclic Filtration Freezing High-Performance Liquid Chromatographies Mass Spectrometry Methylene Chloride methylphenylsulfide Microwaves Peptides Phenol Proteins Resins, Plant Rink amide resin Serine Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Spectrum Analysis Trifluoroacetic Acid Trifluoroethanol Trypsin Vacuum Wang resin
4
Invasion Assay for Plasmodium falciparum
Cited 11 times
P. falciparum asexual stages were maintained in vitro in human O+ erythrocytes at 4% hematocrit in RPMI-1640 media supplemented with 25 mM HEPES, 0.21% sodium bicarbonate, 50 mg/L hypoxanthine, and 0.5% Albumax II. Invasion assays were performed by mixing enzyme-treated infected donor cells with equivalent cell number of RPMI treated erythrocyte control cells, or enzyme-treated erythrocyte negative control cells. Ring-stage parasitized donor cells from the peripheral blood of Senegalese patients were treated with α-2-3,6,8–Vibrio cholera neuraminidase (66.7 mU/ml, Calbiochem), trypsin (1 mg/ml, Sigma), and chymotrypsin (1 mg/ml, Worthington) to prevent reinvasion. Parasites were plated in duplicate at a final parasitemia of between 0.45%-1% at 2% hematocrit in complete RPMI media. Following reinvasion, 48 hours post-plating, parasitemia was assessed by microscopy and by flow cytometry.
Bei A.K., DeSimone T.M., Badiane A.S., Ahouidi A.D., Dieye T., Ndiaye D., Sarr O., Ndir O., Mboup S, & Duraisingh M.T. (2010). A flow cytometry-based assay for measuring invasion of red blood cells by Plasmodium falciparum. American journal of hematology, 85(4), 234-237.
Publication 2010
Bicarbonate, Sodium Biological Assay Blood Cells Cells Chymotrypsin Donor, Blood Enzymes Erythrocytes Flow Cytometry HEPES Homo sapiens Hypoxanthine Microscopy Neuraminidase Parasitemia Parasites Patients Tissue Donors Trypsin Vibrio cholerae Volumes, Packed Erythrocyte
5
Prostate Cancer Screening Protocol in Göteborg, Sweden
Cited 10 times
The design of the Swedish arm of the ERSPC in Göteborg, Sweden, has been previously reported [22 (link)]. In brief, the study population consisted of all males living in Göteborg, Sweden, on 12 December 1994, and who were born between 1 January 1930 and 12 December 1944 (n = 32,298). Of these men, 9972 were randomly selected to undergo initial PSA testing between 1995 and 1996. All men were re-invited for PSA testing every second year up to 2005, unless they were diagnosed with prostate cancer, were aged over 70 or had died. Men with a level of total PSA in serum ≥3.0 ng/ml were invited to undergo clinical examination by an experienced urologist. This examination included digital rectal examination (DRE), and transrectal ultrasound guided laterally directed sextant biopsy of the prostate [23 (link)]. All biopsy specimens were evaluated by a single pathologist. Tumors were classified according to the 1997 International Union Against Cancer staging system [24 ] and graded according to the Gleason grading system [25 ].
Seven milliliters of blood was collected by venipuncture in Vacutainer® tubes from every man who signed informed consent to undergo PSA testing. The blood was allowed to clot, and serum was separated from blood cells by centrifugation at 3000 g for 20 minutes, separated and frozen within 3 hours from collection, and kept frozen at -20°C until analysis. Free and total PSA were measured within 2 weeks from the blood draw by Dr Lilja's laboratory at the Wallenberg Research Laboratories, Department of Laboratory Medicine, Lund University, University Hospital UMAS in Malmö, Sweden, using the dual-label DELFIA Prostatus® total/free PSA-Assay (Perkin-Elmer, Turku, Finland) as reported previously [22 (link)]. During 2005 and 2006, analyses of intact PSA and hK2 were performed at Dr Lilja's laboratory. Samples had been frozen at -20°C for up to 2 years, thawed and aliquoted once, and then stored frozen at -70°C until analysis. All analyses were conducted blind to biopsy result.
The performance of the Prostatus® assay has been comprehensively documented previously [26 (link)]. The combination H117/H50 detects free PSA and PSA bound in complex to 1-anti-chymotrypsin (ACT) in an equimolar fashion [27 (link)], and also fully cross-reacts with hK2 [28 (link)]. The combination of Mabs (monoclonal antibody) H117/5A10 used to measure free PSA does not cross-react with hK2 [28 (link)], or with PSA-ACT (<0.2%) [27 (link)].
Immunodetection of hK2 is based on previously reported in-house research assays [28 (link),29 (link)] where important modifications provide enhanced low-end precision and linearity [30 (link)]. Mab (6H10) has 5% cross-reaction to PSA, but this cross-reaction to PSA is eliminated (0.005%) by the addition of PSA-blocking Mabs (2E9, 2H11, 10, 36). We have previously described the performance of this assay [31 (link)]. Our method for assaying intact PSA has been published [8 (link),17 (link),32 (link)]. Briefly, biotinylated 5A10 antibody is used to capture the free PSA; after incubation and a wash step, we add as detection antibody europium-labeled intact PSA antibody 5C3 that loses binding to PSA when PSA is internally cleaved at Lys145–Lys146. The analytical detection limit of the assay is 0.035 ng/ml.
Vickers A.J., Cronin A.M., Aus G., Pihl C.G., Becker C., Pettersson K., Scardino P.T., Hugosson J, & Lilja H. (2008). A panel of kallikrein markers can reduce unnecessary biopsy for prostate cancer: data from the European Randomized Study of Prostate Cancer Screening in Göteborg, Sweden. BMC Medicine, 6, 19.
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Publication 2008
Biological Assay Biopsy Blindness BLOOD Blood Cells Centrifugation Childbirth Chymotrypsin Clotrimazole Cross Reactions Digital Rectal Examination Europium Freezing Immunoglobulins menthyl 3-(2-pyridylsulfinyl)acrylate Monoclonal Antibodies Neoplasms Pathologists Pharmaceutical Preparations Phlebotomy Physical Examination Prostate Prostate Cancer Serum Ultrasonography Urologists

Most recents protocols related to «Chymotrypsin»

1
Proteomic Analysis of Lysosomal Enzymes
25 µg of purified AGA, GUSB CTSD, and GAA were dissolved in 50 mM ammonium bicarbonate (AmBic) buffer (pH 7.4) and further reduced with 10 mM dithiothreitol (DTT) at 60°C for 45 min on shaker, followed by alkylation with 20 mM iodoacetamide (IAA) at 25°C for 30 min in darkness. AGA, GUSB, CTSD were subjected to proteolytic digestion with chymotrypsin (1:40 enzyme-substrate ratio), while GAA was digested in gel with trypsin (1:25 enzyme-substrate ratio) after SDS-PAGE separation. The reaction was quenched with 1 µL trifluoroacetic acid (TFA) and the digested sample was desalted by custom-made modified StageTip colums with three layers of C18 and two layers of C8 membrane (3 M Empore disks, Sigma-Aldrich). Samples were eluted with two steps of 50 µL 50% methanol in 0.1% formic acid. Final sample was aliqoted in two equal parts. The first aliquot was placed into a glass insert (Agilent), dried completely in SpeedVac (Eppendorf) and further re-dissolved in 50 µL 0.1% formic acid (FA) and submitted for nLC-MS analysis. The second aliqout was placed inside an Eppendorf tube, dried completely using SpeedVac, and then re-dissolved in 50 µL of 50 mM AmBic buffer (pH 7.4) and incubated with PNGase F (1U per sample) for 12 h with shaking at 37°C. Samples treated with PNGase F were desalted and dried using the same methods mentioned above for the first aliqout and submitted for nLC-MS/MS analysis.
Chen Y.H., Tian W., Yasuda M., Ye Z., Song M., Mandel U., Kristensen C., Povolo L., Marques A.R., Čaval T., Heck A.J., Sampaio J.L., Johannes L., Tsukimura T., Desnick R., Vakhrushev S.Y., Yang Z, & Clausen H. (2023). A universal GlycoDesign for lysosomal replacement enzymes to improve circulation time and biodistribution. Frontiers in Bioengineering and Biotechnology, 11, 1128371.
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Publication 2023
Alkylation ammonium bicarbonate Buffers Chymotrypsin CTSD protein, human Darkness Digestion Dithiothreitol Empore Enzymes formic acid Glycopeptidase F Iodoacetamide Methanol Peptide Hydrolases SDS-PAGE Tandem Mass Spectrometry Tissue, Membrane Trifluoroacetic Acid Trypsin
2
In vitro Digestion of Cooked Chicken Muscle
For in vitro digestion, the ground chicken muscles were
vacuum-packed and cooked at 80°C to reach a core temperature of
75°C, followed by cooling to 25°C. Cooked samples were chopped to
simulate mastication.
The elderly in vitro digestion model herein was designed based
on previous studies by Hernández-Olivas
et al. (2020) and Minekus et al.
(2014). All the digestive enzymes that were used herein were
purchased from Sigma-Aldrich (St. Louis, MO, USA). The simulated salivary fluid
(pH 7.0), gastric fluid (pH 6.0), and duodenal fluid (pH 7.0) contained 75 U/mL
α-amylase from Aspergillus oryzae (EC 3.2.1.1), 1,500
U/mL pepsin from Porcine mucosa (EC 3.4.23.1), 50 U/mL trypsin
(EC 3.4.21.4) and 12.5 U/mL chymotrypsin (EC 3.4.21.1) from bovine pancreas,
1,000 U/mL pancreatic lipase from porcine pancreas (EC 3.1.1.3), and 5 mM
porcine bile extract (EC 232-369-0). Digestive fluid was mixed with the digesta
from the previous compartment at 50:50 (vol/vol) during digestion. Each
digestion was conducted for 120 min at 37°C and a rotational speed of 100
rpm, except for oral digestion, which was conducted for 2 min. All digesta
samples were stored at −70°C until analysis, immediately after
digestion. Control samples were prepared for digestion under the same conditions
through addition of distilled water instead of meat samples to exclude protein
content from the digestive enzymes.
Herein, the size fractionation of the digesta was conducted to determine protein
digestibility after in vitro digestion. After sequential
filtration using a centrifugal filter with molecular weight cut-offs of 10 and 3
kDa (Amicon Ultra-15, Millipore, Billerica, MA, USA) according to the
manufacturer’s protocol, the protein content of the filtrate and whole
digesta was measured using the Kjeldahl method to represent the amount of
protein digested under 3 kDa. Protein digestibility was calculated using the
following Eq. (1):
Lee S., Jo K., Jeong H.G., Jeong S.K., Park J.I., Yong H.I., Choi Y.S, & Jung S. (2023). Higher Protein Digestibility of Chicken Thigh than Breast Muscle in an In Vitro Elderly Digestion Model. Food Science of Animal Resources, 43(2), 305-318.
Publication 2023
Aged Amylase Aspergillus oryzae Bile Bos taurus Chewing Chickens Chymotrypsin Digestion Duodenum Enzymes Fractionation, Chemical Lipase Meat Mucous Membrane Muscle Tissue Pancreas Pepsin A Pigs Proteins Stomach Trypsin
3
Protein Identification by Mass Spectrometry
In gel reduction, alkylation, and digestion with trypsin or chymotrypsin were performed on the gel sample prior to subsequent analysis by mass spectrometry. Cysteine residues were reduced with dithiothreitol and were derivatized by treatment with iodoacetamide to form stable carbamidomethyl derivatives. Trypsin digestion was carried out overnight at room temperature after initial incubation at 37 °C for 2 h.
Sample digests, resuspended in 0.1% (v/v) formic acid, were analyzed by online nano-flow reverse-phase high-performance LC with online electrospray-MS analysis with MS/MS (MSe) using a Waters SYNAPT G2-S high-definition mass spectrometer, which was coupled to a Waters ACQUITY UPLC M-Class System (Waters UK, Elstree). Separations were achieved by means of a C18 trapping column (M-Class Symmetry C18 Trap, 100 Å, 5 μm, 180 μm × 20 mm, 2G) connected in line with a 75-μm C18 reverse-phase analytical column (M-Class Peptide BEH C18, 130 Å, 1.7 μm, 75 μm × 150 mm), eluted over 90 min with a gradient of acetonitrile in 0.1% formic acid at a flow rate of 300 nL/min. Column temperatures were maintained at 50 °C, and data were recorded in MSe “Resolution”-positive ion mode, with scan times set to 0.5 s in both the high-energy and low-energy modes of operation. The instrument was precalibrated using 10–100 fmol/μL of [Glu1]-fibrinopeptide B/5% (v/v) acetic acid (1:3, v/v) and was calibrated during analysis by means of a lockmass system using [Glu1]-Fibrinopeptide B 785.84262+ ion. The collision gas utilized was argon with collision energy ramp of 20–45 eV. Data acquisition was performed using MassLynx (Waters UK, Elstree) software and data were analyzed by means of MassLynx, BiopharmaLynx and PLGS version 3.0.2 (Waters UK, Elstree).
Passmore I.J., Faulds-Pain A., Abouelhadid S., Harrison M.A., Hall C.L., Hitchen P., Dell A., Heap J.T, & Wren B.W. (2023). A combinatorial DNA assembly approach to biosynthesis of N-linked glycans in E. coli. Glycobiology, 33(2), 138-149.
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Publication 2023
Acetic Acid acetonitrile Alkylation Argon Chymotrypsin Cysteine derivatives Digestion Dithiothreitol Fibrinopeptide B formic acid Iodoacetamide Mass Spectrometry Peptides Radionuclide Imaging Tandem Mass Spectrometry Trypsin
4
SARS-CoV-2 Spike Protein Purification
Purified SARS-CoV-2 spike antigen (S1-RBD) [His-Tag (HEK293)] was purchased from the Native Antigen Company [REC31882-500].
Tris-HCl was from Invitrogen. Dithiothreitol (DTT), iodoacetamide (IAM) and urea were from Sigma-Aldrich, digestion enzymes endoproteinase Lys-C and chymotrypsin from Thermo Scientific and MS grade formic acid and acetonitrile from Biosolve.
Frans G., Dillaerts D., Dehaemers T., Van Elslande J., De Leeuw J., Boon L., Maes W., Callewaert N., Calcoen B., Ancheva L., Cockx M., Geukens N., Arat K., Derua R., Vermeersch P., Carpentier S.C, & Bossuyt X. (2023). Complementarity determining regions in SARS-CoV-2 hybrid immunity. Frontiers in Immunology, 14, 1050037.
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Publication 2023
acetonitrile Antigens Chymotrypsin Digestion Dithiothreitol Enzymes formic acid Iodoacetamide peptidyl-Lys metalloendopeptidase SARS-CoV-2 Tromethamine Urea
5
Dual-Enzyme Protein Digestion Protocol
Following enrichment, 60 µl 4 M urea/50 mM Tris-HCl was added to each well. Afterwards, reduction of proteins was executed for 1h in the thermomixer (800 rpm, 37°C) in the presence of 8 mM DTT, followed by alkylation for 30 min in the dark (37°C) in the presence of 22 mM IAM. Digestion was started by addition of Lys-C at 0,4 µg/well and left overnight (thermomixer 37°C, 800 rpm, dark). The next day, 50 mM Tris-HCl was added until urea concentration dropped below 1 M. Chymotrypsin was added at 1 µg/well and digestion of the proteins continued in the thermomixer (4 h, 37°C, 800 rpm). Finally, digestion was stopped in the presence of 1% FA.
Frans G., Dillaerts D., Dehaemers T., Van Elslande J., De Leeuw J., Boon L., Maes W., Callewaert N., Calcoen B., Ancheva L., Cockx M., Geukens N., Arat K., Derua R., Vermeersch P., Carpentier S.C, & Bossuyt X. (2023). Complementarity determining regions in SARS-CoV-2 hybrid immunity. Frontiers in Immunology, 14, 1050037.
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Publication 2023
Alkylation Chymotrypsin Digestion Protein Digestion Proteins Tromethamine Urea

Top products related to «Chymotrypsin»

1
Chymotrypsin by Merck Group
Sourced in United States, Germany, Canada, Italy, China, Belgium
Chymotrypsin is a digestive enzyme produced by the pancreas. It is commonly used in laboratory settings to break down proteins into smaller peptides or amino acids. Chymotrypsin acts by hydrolyzing peptide bonds on the carbonyl side of aromatic amino acid residues, such as tyrosine, tryptophan, and phenylalanine.
2
Trypsin by Merck Group
Sourced in United States, Germany, United Kingdom, China, Italy, Japan, Sao Tome and Principe, Canada, Macao, Poland, India, France, Spain, Portugal, Australia, Switzerland, Ireland, Belgium, Sweden, Israel, Brazil, Czechia, Denmark, Austria
Trypsin is a serine protease enzyme that is commonly used in cell biology and biochemistry laboratories. Its primary function is to facilitate the dissociation and disaggregation of adherent cells, allowing for the passive release of cells from a surface or substrate. Trypsin is widely utilized in various cell culture applications, such as subculturing and passaging of adherent cell lines.
3
α chymotrypsin by Merck Group
Sourced in United States, Germany, China
α-chymotrypsin is a digestive enzyme produced by the pancreas. It is commonly used in biochemistry and molecular biology research laboratories for its ability to cleave peptide bonds in proteins.
4
Chymotrypsin by Promega
Sourced in United States, Australia, Italy, United Kingdom
Chymotrypsin is a proteolytic enzyme derived from bovine pancreas. It is commonly used in biochemical and molecular biology applications to cleave peptide bonds following aromatic amino acid residues, such as tyrosine, tryptophan, and phenylalanine.
5
Trypsin by Promega
Sourced in United States, Germany, United Kingdom, China, Japan, France, Switzerland, Sweden, Italy, Netherlands, Spain, Canada, Brazil, Australia, Macao
Trypsin is a serine protease enzyme that is commonly used in cell culture and molecular biology applications. It functions by cleaving peptide bonds at the carboxyl side of arginine and lysine residues, which facilitates the dissociation of adherent cells from cell culture surfaces and the digestion of proteins.
6
Pepsin by Merck Group
Sourced in United States, Germany, China, United Kingdom, Italy, Poland, France, Sao Tome and Principe, Spain, Canada, India, Australia, Ireland, Switzerland, Sweden, Japan, Macao, Israel, Singapore, Denmark, Argentina, Belgium
Pepsin is a proteolytic enzyme produced by the chief cells in the stomach lining. It functions to break down proteins into smaller peptides during the digestive process.
7
Chymotrypsin by Roche
Sourced in Germany, United States, Switzerland
Chymotrypsin is a pancreatic enzyme that catalyzes the hydrolysis of peptide bonds in proteins. It is commonly used in laboratory settings for protein digestion and analysis.
8
Iodoacetamide by Merck Group
Sourced in United States, Germany, United Kingdom, Sao Tome and Principe, Italy, France, Macao, China, Canada, Australia, Switzerland, Spain
Iodoacetamide is a chemical compound commonly used in biochemistry and molecular biology laboratories. It is a reactive compound that selectively modifies cysteine residues in proteins, thereby allowing for the study of protein structure and function. Iodoacetamide is often used in sample preparation procedures for mass spectrometry and other analytical techniques.
9
Dithiothreitol (dtt) by Merck Group
Sourced in United States, Germany, United Kingdom, Italy, Sao Tome and Principe, France, China, Switzerland, Macao, Spain, Australia, Canada, Belgium, Sweden, Brazil, Austria, Israel, Japan, New Zealand, Poland, Bulgaria
Dithiothreitol (DTT) is a reducing agent commonly used in biochemical and molecular biology applications. It is a small, water-soluble compound that helps maintain reducing conditions and prevent oxidation of sulfhydryl groups in proteins and other biomolecules.
10
Proteinase k by Merck Group
Sourced in United States, Germany, United Kingdom, Italy, Japan, Sao Tome and Principe, Canada, Belgium, Macao, Australia, Israel, France, China, Czechia, Singapore, Norway, Austria, Switzerland, Spain
Proteinase K is a serine protease enzyme that is commonly used in molecular biology and biochemistry laboratories. It is a highly active enzyme that efficiently digests a wide range of proteins, including those found in cell membranes, cytoplasmic proteins, and nuclear proteins. Proteinase K is known for its ability to effectively inactivate DNases and RNases, making it a valuable tool for the purification and isolation of nucleic acids.

More about "Chymotrypsin"

Chymotrypsin is a critical serine protease enzyme found in the pancreas and gastrointestinal tract.
It plays a vital role in the digestion of dietary proteins, catalyzing the hydrolysis of peptide bonds, particularly on the carboxy side of aromatic amino acids like tyrosine, tryptophan, and phenylalanine.
This process breaks down larger proteins into smaller peptides and amino acids for absorption.
The activity of chymotrypsin is regulated by other pancreatic enzymes, such as trypsin and α-chymotrypsin, and can be inhibited by certain compounds like iodoacetamide and dithiothreitol.
Understanding the structure, function, and regulation of chymotrypsin is crucial for research on digestive processes and related disorders, including enzyme-related conditions like pancreatitis and maldigestion.
Researchers can leverage the insights from chymotrypsin's MeSH term description to optimize their experiments and streamline their research.
Tools like PubCompare.ai's AI-powered platform can help scientists quickly locate the best protocols from literature, preprints, and patents, enabling them to make informed decisions and enhance their chymotrypsin-related studies.
By incorporating related terms, abbreviations, and key subtopics, researchers can gain a comprehensive understanding of chymotrypsin and its role in digestion and related fields of study.