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TrypsinTrypsin Inhibitor, Kazal PancreaticTrypsin Inhibitor, Kunitz SoybeanChymotrypsinTrypsin Inhibitor, Bowman-Birk SoybeanAprotininTrypsinogenAmino Acid SequenceReceptor, PAR-2Peptide FragmentsMolecular Sequence DataMolecular WeightPeptide HydrolasesProtease InhibitorsCattleKineticsPancreasEndopeptidasesBenzoylarginine NitroanilideSerine Proteinase InhibitorsSerine EndopeptidasesBinding SitesBenzamidinesAmino AcidsProtein ConformationHydrolysisPancreatic ElastaseChromatography, GelPronaseThermolysinHydrogen-Ion Concentrationalpha-MacroglobulinsPapainCyanogen BromideOvomucinPepsin AChromatography, High Pressure LiquidPeptide MappingReceptors, ThrombinStreptomyces griseusProtein BindingDisulfidesPancreatic JuicePlant ProteinsAmylasesTosylarginine Methyl Esteralpha 1-AntitrypsinKallikreinsCarboxypeptidases APeptidesCarboxypeptidasesEnzyme PrecursorsGlycoproteinsFibrinolysinSubstrate SpecificityMacromolecular SubstancesChemistrySwineChemical PhenomenaHot TemperatureModels, MolecularEnzymes, ImmobilizedCell MembraneChymotrypsinogenIntestinal SecretionsChromatography, AffinityRabbitsGabexateThrombinPancreatitisSoybeansRecombinant ProteinsSeedsMicrobial CollagenaseSequence Homology, Amino AcidEscherichia coliOligopeptidesChromatography, Ion ExchangeAcrosinReceptor, PAR-1Cell LineStructure-Activity RelationshipEnzyme ActivationTemperatureMass SpectrometryCucurbitaceaeBase Sequence
Trypsin
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.
Trypsin Inhibitor, Kazal Pancreatic
A pancreatic trypsin inhibitor common to all mammals. It is secreted with the zymogens into the pancreatic juice. It is a protein composed of 56 amino acid residues and is different in amino acid composition and physiological activity from the Kunitz bovine pancreatic trypsin inhibitor (APROTININ).
Trypsin Inhibitor, Kunitz Soybean
A high-molecular-weight protein (approximately 22,500) containing 198 amino acid residues. It is a strong inhibitor of trypsin and human plasmin.
Chymotrypsin
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.
Trypsin Inhibitor, Bowman-Birk Soybean
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.
Aprotinin
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)
Trypsinogen
The inactive proenzyme of trypsin secreted by the pancreas, activated in the duodenum via cleavage by enteropeptidase. (Stedman, 25th ed)
Amino Acid Sequence
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.
Receptor, PAR-2
A G-protein-coupled, proteinase-activated receptor that is expressed in a variety of tissues including ENDOTHELIUM; LEUKOCYTES; and the GASTROINTESTINAL TRACT. The receptor is activated by TRYPSIN, which cleaves off the N-terminal peptide from the receptor. The new N-terminal peptide is a cryptic ligand for the receptor. The uncleaved receptor can also be activated by the N-terminal peptide present on the activated THROMBIN RECEPTOR and by small synthetic peptides that contain the unmasked N-terminal sequence.
Peptide Fragments
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Molecular Sequence Data
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.
Molecular Weight
The sum of the weight of all the atoms in a molecule.
Peptide Hydrolases
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Protease Inhibitors
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
Cattle
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.
Kinetics
The rate dynamics in chemical or physical systems.
Pancreas
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.
Endopeptidases
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Benzoylarginine Nitroanilide
A chromogenic substrate that permits direct measurement of peptide hydrolase activity, e.g., papain and trypsin, by colorimetry. The substrate liberates p-nitroaniline as a chromogenic product.
Serine Proteinase Inhibitors
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
Serine Endopeptidases
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
Binding Sites
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Benzamidines
Amidines substituted with a benzene group. Benzamidine and its derivatives are known as peptidase inhibitors.
Amino Acids
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.
Protein Conformation
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).
Hydrolysis
The process of cleaving a chemical compound by the addition of a molecule of water.
Pancreatic Elastase
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.
Chromatography, Gel
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
Pronase
A proteolytic enzyme obtained from Streptomyces griseus.
Thermolysin
A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.
Hydrogen-Ion Concentration
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)
alpha-Macroglobulins
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.
Papain
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.
Cyanogen Bromide
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.
Ovomucin
A heterogeneous mixture of glycoproteins responsible for the gel structure of egg white. It has trypsin-inhibiting activity.
Pepsin A
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.
Chromatography, High Pressure Liquid
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Peptide Mapping
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.
Receptors, Thrombin
A family of proteinase-activated receptors that are specific for THROMBIN. They are found primarily on PLATELETS and on ENDOTHELIAL CELLS. Activation of thrombin receptors occurs through the proteolytic action of THROMBIN, which cleaves the N-terminal peptide from the receptor to reveal a new N-terminal peptide that is a cryptic ligand for the receptor. The receptors signal through HETEROTRIMERIC GTP-BINDING PROTEINS. Small synthetic peptides that contain the unmasked N-terminal peptide sequence can also activate the receptor in the absence of proteolytic activity.
Streptomyces griseus
An actinomycete from which the antibiotics STREPTOMYCIN, grisein, and CANDICIDIN are obtained.
Protein Binding
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.
Disulfides
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
Pancreatic Juice
The fluid containing digestive enzymes secreted by the pancreas in response to food in the duodenum.
Plant Proteins
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
Amylases
A group of amylolytic enzymes that cleave starch, glycogen, and related alpha-1,4-glucans. (Stedman, 25th ed) EC 3.2.1.-.
Tosylarginine Methyl Ester
Arginine derivative which is a substrate for many proteolytic enzymes. As a substrate for the esterase from the first component of complement, it inhibits the action of C(l) on C(4).
alpha 1-Antitrypsin
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.
Kallikreins
Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increase vascular permeability and affect smooth muscle. They act as infertility agents in men. Three forms are recognized, PLASMA KALLIKREIN (EC 3.4.21.34), TISSUE KALLIKREIN (EC 3.4.21.35), and PROSTATE-SPECIFIC ANTIGEN (EC 3.4.21.77).
Carboxypeptidases A
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.
Peptides
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.
Carboxypeptidases
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
Enzyme Precursors
Physiologically inactive substances that can be converted to active enzymes.
Glycoproteins
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
Fibrinolysin
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.
Substrate Specificity
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Macromolecular Substances
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.
Chemistry
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
Swine
Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).
Chemical Phenomena
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
Hot Temperature
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
Models, Molecular
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Enzymes, Immobilized
Enzymes which are immobilized on or in a variety of water-soluble or water-insoluble matrices with little or no loss of their catalytic activity. Since they can be reused continuously, immobilized enzymes have found wide application in the industrial, medical and research fields.
Cell Membrane
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Chymotrypsinogen
Intestinal Secretions
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.
Chromatography, Affinity
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)
Rabbits
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
Gabexate
A serine proteinase inhibitor used therapeutically in the treatment of pancreatitis, disseminated intravascular coagulation (DIC), and as a regional anticoagulant for hemodialysis. The drug inhibits the hydrolytic effects of thrombin, plasmin, and kallikrein, but not of chymotrypsin and aprotinin.
Thrombin
An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN.
Pancreatitis
INFLAMMATION of the PANCREAS. Pancreatitis is classified as acute unless there are computed tomographic or endoscopic retrograde cholangiopancreatographic findings of CHRONIC PANCREATITIS (International Symposium on Acute Pancreatitis, Atlanta, 1992). The two most common forms of acute pancreatitis are ALCOHOLIC PANCREATITIS and gallstone pancreatitis.
Soybeans
An annual legume. The SEEDS of this plant are edible and used to produce a variety of SOY FOODS.
Recombinant Proteins
Proteins prepared by recombinant DNA technology.
Seeds
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.
Microbial Collagenase
A metalloproteinase which degrades helical regions of native collagen to small fragments. Preferred cleavage is -Gly in the sequence -Pro-Xaa-Gly-Pro-. Six forms (or 2 classes) have been isolated from Clostridium histolyticum that are immunologically cross-reactive but possess different sequences and different specificities. Other variants have been isolated from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio and Streptomyces. EC 3.4.24.3.
Sequence Homology, Amino Acid
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Escherichia coli
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Oligopeptides
Peptides composed of between two and twelve amino acids.
Chromatography, Ion Exchange
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.
Acrosin
A trypsin-like enzyme of spermatozoa which is not inhibited by alpha 1 antitrypsin.
Receptor, PAR-1
A thrombin receptor subtype that couples to HETEROTRIMERIC GTP-BINDING PROTEINS resulting in the activation of a variety of signaling mechanisms including decreased intracellular CYCLIC AMP, increased TYPE C PHOSPHOLIPASES and increased PHOSPHOLIPASE A2.
Cell Line
Established cell cultures that have the potential to propagate indefinitely.
Structure-Activity Relationship
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.
Enzyme Activation
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Temperature
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
Mass Spectrometry
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
Cucurbitaceae
The gourd plant family of the order Violales, subclass Dilleniidae, class Magnoliopsida. It is sometimes placed in its own order, Cucurbitales. 'Melon' generally refers to CUCUMIS; CITRULLUS; or MOMORDICA.
Base Sequence
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. The tryptic peptides. (1/9857)

The NADP-specific glutamate dehydrogenase of Neurospora crassa was digested with trypsin, and peptides accounting for 441 out of the 452 residues of the polypeptide chain were isolated and substantially sequenced. Additional experimental detail has been deposited as Supplementary Publication SUP 50052 (11 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)

The effects of digestive enzymes on characteristics of placental insulin receptor. Comparison of particulate and soluble receptor preparations. (2/9857)

The role of the surrounding membrane structure on the binding characteristics of the insulin receptor was studied by using several digestive enzymes. The effects observed with particulate membrane preparations are compared with those from soluble receptor preparations. beta-Galactosidase and neuraminidase had no effect on insulin binding to either particulate or soluble receptors from human placentae. Exposure to 2 units of phospholipase C/ml increased insulin binding to particulate membranes, but was without effect on the soluble receptor preparation. The increase in binding to particulate membranes was shown to be due to an increase in apparent receptor number. After 5 min exposure to 500 microgram of trypsin/ml there was an increase in insulin binding to the particulate membrane fraction, owing to an increase in receptor affinity. After 15 min exposure to this amount of trypsin, binding decreased, owing to a progressive decrease in receptor availability. In contrast, this concentration of trypsin had no effect on the solubilized receptor preparation. Because of the differential effects of phospholipase C and trypsin on the particulate compared with the solubilized receptor preparations, it is concluded that the effects of these enzymes were due to an effect on the surrounding membrane structure. Changes in receptor configuration due to alterations within the adjoining membrane provide a potential mechanism for mediating short-term alterations in receptor function.  (+info)

Stable remodeling of tailless nucleosomes by the human SWI-SNF complex. (3/9857)

The histone N-terminal tails have been shown previously to be important for chromatin assembly, remodeling, and stability. We have tested the ability of human SWI-SNF (hSWI-SNF) to remodel nucleosomes whose tails have been cleaved through a limited trypsin digestion. We show that hSWI-SNF is able to remodel tailless mononucleosomes and nucleosomal arrays, although hSWI-SNF remodeling of tailless nucleosomes is less effective than remodeling of nucleosomes with tails. Analogous to previous observations with tailed nucleosomal templates, we show both (i) that hSWI-SNF-remodeled trypsinized mononucleosomes and arrays are stable for 30 min in the remodeled conformation after removal of ATP and (ii) that the remodeled tailless mononucleosome can be isolated on a nondenaturing acrylamide gel as a novel species. Thus, nucleosome remodeling by hSWI-SNF can occur via interactions with a tailless nucleosome core.  (+info)

The C-terminal region of hPrp8 interacts with the conserved GU dinucleotide at the 5' splice site. (4/9857)

A U5 snRNP protein, hPrp8, forms a UV-induced crosslink with the 5' splice site (5'SS) RNA within splicing complex B assembled in trans- as well as in cis-splicing reactions. Both yeast and human Prp8 interact with the 5'SS, branch site, polypyrimidine tract, and 3'SS during splicing. To begin to define functional domains in Prp8 we have mapped the site of the 5'SS crosslink within the hPrp8 protein. Immunoprecipitation analysis limited the site of crosslink to the C-terminal 5060-kDa segment of hPrp8. In addition, size comparison of the crosslink-containing peptides generated with different proteolytic reagents with the pattern of fragments predicted from the hPrp8 sequence allowed for mapping of the crosslink to a stretch of five amino acids in the C-terminal portion of hPrp8 (positions 1894-1898). The site of the 5'SS:hPrp8 crosslink falls within a segment spanning the previously defined polypyrimidine tract recognition domain in yPrp8, suggesting that an overlapping region of Prp8 may be involved both in the 5'SS and polypyrimidine tract recognition events. In the context of other known interactions of Prp8, these results suggest that this protein may participate in formation of the catalytic center of the spliceosome.  (+info)

Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. (5/9857)

Misfolded or unassembled secretory proteins are retained in the endoplasmic reticulum (ER) and subsequently degraded by the cytosolic ubiquitin-proteasome system. This requires their retrograde transport from the ER lumen into the cytosol, which is mediated by the Sec61 translocon. It had remained a mystery whether ER-localised soluble proteins are at all capable of re-entering the Sec61 channel de novo or whether a permanent contact of the imported protein with the translocon is a prerequisite for retrograde transport. In this study we analysed two new variants of the mutated yeast carboxypeptidase yscY, CPY*: a carboxy-terminal fusion protein of CPY* and pig liver esterase and a CPY* species carrying an additional glycosylation site at its carboxy-terminus. With these constructs it can be demonstrated that the newly synthesised CPY* chain is not retained in the translocation channel but reaches its ER lumenal side completely. Our data indicate that the Sec61 channel provides the essential pore for protein transport through the ER membrane in either direction; persistent contact with the translocon after import seems not to be required for retrograde transport.  (+info)

Reaction specificity of native and nicked 3,4-dihydroxyphenylalanine decarboxylase. (6/9857)

3,4-Dihydroxyphenylalanine (Dopa) decarboxylase is a stereospecific pyridoxal 5'-phosphate (PLP)-dependent alpha-decarboxylase that converts L-aromatic amino acids into their corresponding amines. We now report that reaction of the enzyme with D-5-hydroxytryptophan or D-Dopa results in a time-dependent inactivation and conversion of the PLP coenzyme to pyridoxamine 5'-phosphate and PLP-D-amino acid Pictet-Spengler adducts, which have been identified by high performance liquid chromatography. We also show that the reaction specificity of Dopa decarboxylase toward aromatic amines depends on the experimental conditions. Whereas oxidative deamination occurs under aerobic conditions (Bertoldi, M., Moore, P. S., Maras, B., Dominici, P., and Borri Voltattorni, C. (1996) J. Biol. Chem. 271, 23954-23959; Bertoldi, M., Dominici, P., Moore, P. S., Maras, B., and Borri Voltattorni, C. (1998) Biochemistry 37, 6552-6561), half-transamination and Pictet-Spengler reactions take place under anaerobic conditions. Moreover, we examined the reaction specificity of nicked Dopa decarboxylase, obtained by selective tryptic cleavage of the native enzyme between Lys334 and His335. Although this enzymatic species does not exhibit either decarboxylase or oxidative deamination activities, it retains a large percentage of the native transaminase activity toward D-aromatic amino acids and displays a slow transaminase activity toward aromatic amines. These transamination reactions occur concomitantly with the formation of cyclic coenzyme-substrate adducts. Together with additional data, we thus suggest that native Dopa decarboxylase can exist as an equilibrium among "open," "half-open," and "closed" forms.  (+info)

Enrichment of enzyme activity on deformylation of 1-NFK-lysozyme. (7/9857)

The formamide linkage of an inactive lysozyme derivative (1-NFK-lysozyme), formed by selective ozonization of tryptophan 62 in hen egg-white lysozyme [EC 3.2.1.17] was hydrolyzed with dilute acid faster in the frozen state at about --10 degrees than at 20 degrees. On hydrolysis of 1-NFK-lysozyme the low lytic activity increased to approximately 80% of that of native lysozyme. It is suggested that the binding ability associated with kynurenine 62 in the lysozyme derivative formed by this hydrolysis may be responsible for increase in enzymatic activity.  (+info)

Further studies on the mechanism of adrenaline-induced lipolysis in lipid micelles. (8/9857)

Lipase [EC 3.1.1.3] depleted lipid micelles, in which lipolysis was not elicited by adrenaline, were prepared from lipid micelles. When these lipase-depleted lipid micelles incubated with adipose tissue extract containing lipase activity, adrenaline-induced lipolysis was restored to almost the same level as that of native lipid micelles. Adrenaline-induced lipolysis was not restored when the lipase-depleted lipid micelles were homogenized or sonicated. Various tissue extracts from kidney, lung, liver, and pancreas, and post-heparin plasma, which contained lipase activity, restored adrenaline-induced lipolysis in lipase-depleted lipid micelles.  (+info)

Pancreatitis is inflammation of the pancreas. The pancreas is a gland located behind the stomach that produces digestive enzymes and hormones. Pancreatitis can be acute, meaning it occurs suddenly and resolves quickly, or chronic, meaning it persists over time.

There are several causes of pancreatitis, including:

1. Gallstones: These can block the pancreatic duct, causing inflammation.
2. Alcohol consumption: Heavy alcohol use can damage the pancreas and lead to inflammation.
3. High triglycerides: Elevated levels of triglycerides in the blood can cause pancreatitis.
4. Infections: Viral or bacterial infections can infect the pancreas and cause inflammation.
5. Genetic factors: Some people may be more susceptible to pancreatitis due to inherited genetic mutations.
6. Pancreatic trauma: Physical injury to the pancreas can cause inflammation.
7. Certain medications: Some medications, such as certain antibiotics and chemotherapy drugs, can cause pancreatitis as a side effect.

Symptoms of pancreatitis may include:

1. Abdominal pain
2. Nausea and vomiting
3. Fever
4. Diarrhea or bloating
5. Weight loss
6. Loss of appetite

Treatment for pancreatitis depends on the underlying cause and the severity of the condition. In some cases, hospitalization may be necessary to manage symptoms and address any complications. Treatment options may include:

1. Pain management: Medications such as nonsteroidal anti-inflammatory drugs (NSAIDs) or opioids may be used to manage abdominal pain.
2. Fluid replacement: Intravenous fluids may be given to replace lost fluids and electrolytes.
3. Antibiotics: If the pancreatitis is caused by an infection, antibiotics may be prescribed to treat the infection.
4. Nutritional support: Patients with pancreatitis may require nutritional support to ensure they are getting enough calories and nutrients.
5. Pancreatic enzyme replacement therapy: In some cases, pancreatic enzyme replacement therapy may be necessary to help the body digest food.
6. Surgery: In severe cases of pancreatitis, surgery may be necessary to remove damaged tissue or repair damaged blood vessels.

It is important to seek medical attention if you experience persistent abdominal pain or other symptoms of pancreatitis, as early treatment can help prevent complications and improve outcomes.

TrypsinTrypsin
... 1 S01.151, Trypsin 2 S01.258, Trypsin 3 S01.174 Trypsin Inhibitors and Trypsin Assay Method at Sigma-Aldrich Trypsin at ... Cod trypsins include trypsin I with an activity range of 4 to 65 °C (40 to 150 °F) and maximal activity at 55 °C (130 °F), as ... Trypsin can also be used to dissociate dissected cells (for example, prior to cell fixing and sorting). Trypsin can be used to ... Human trypsin has an optimal operating temperature of about 37 °C. In contrast, the Atlantic cod has several types of trypsins ...
https://en.wikipedia.org/wiki/Trypsin
Trypsin 1Trypsin 1
Trypsin-1 is the main isoform of trypsinogen secreted by pancreas, the others are trypsin-2 (anionic trypsinogen), and trypsin- ... Arg 117 is a trypsin-sensitive site which can be cleaved by another trypsin and becomes inactivated. This site may be a fail- ... Trypsin-1, also known as cationic trypsinogen, is a protein that in humans is encoded by the PRSS1 gene. ... Kimland M, Russick C, Marks WH, Borgström A (1990). "Immunoreactive anionic and cationic trypsin in human serum". Clin. Chim. ...
https://en.wikipedia.org/wiki/Trypsin_1
Trypsin inhibitorTrypsin inhibitor
"The role of trypsin, trypsin inhibitor and trypsin receptor in the onset and aggravation of pancreatitis". Journal of ... Trypsin inhibitor can also be essential for biological processes within the plant. Trypsin inhibitor can also naturally occur ... Therefore, trypsin inhibitors are considered an anti-nutritional factor or ANF. Additionally, trypsin inhibitor partially ... Additionally, pancreatic hypertrophy is a common occurrence with trypsin inhibitor consumption The presence of trypsin ...
https://en.wikipedia.org/wiki/Trypsin_inhibitor
Sunflower trypsin inhibitorSunflower trypsin inhibitor
One example of Sunflower trypsin inhibitor is Sunflower trypsin inhibitor-1 (SFTI-1). Sunflower trypsin inhibitor-1 is a potent ... By modifying the amino acid sequence of sunflower trypsin inhibitor, more specifically, sunflower trypsin inhibitor-1 (SFTI-1 ... Sunflower trypsin inhibitor-1 is the simplest cysteine-rich peptide scaffold because it is a bicyclic 14 amino acid peptide and ... Sunflower trypsin inhibitor (SFTI) is a small, circular peptide produced in sunflower seeds, and is a potent inhibitor of ...
https://en.wikipedia.org/wiki/Sunflower_trypsin_inhibitor
Inter-alpha-trypsin inhibitorInter-alpha-trypsin inhibitor
... s (IαI) are plasma proteins consisting of three of four heavy chains selected from the group ITIH1 ... Zhuo L, Hascall VC, Kimata K (September 2004). "Inter-alpha-trypsin inhibitor, a covalent protein-glycosaminoglycan-protein ...
https://en.wikipedia.org/wiki/Inter-alpha-trypsin_inhibitor
EnteropeptidaseEnteropeptidase
Kunitz M, Northrop JH (Jul 20, 1936). "Isolation from beef pancreas of crystalline trypsinogen, trypsin, a trypsin inhibitor, ... Enteropeptidase exhibits trypsin-like activity, cleaving proteins following a lysine at a specific cleavage site (Asp-Asp-Asp- ... Kiel B (1971). "Trypsin". In Boyer PS (ed.). The Enzymes, 3: Hydrolysis - Peptide Bonds. Amsterdam: Elsevier. pp. 249-75. ISBN ... Lu D, Yuan X, Zheng X, Sadler JE (December 12, 1997). "Bovine proenteroptidase is activated by trypsin, and the specificity of ...
https://en.wikipedia.org/wiki/Enteropeptidase
Enzyme inhibitorEnzyme inhibitor
Many of these are activated by the trypsin protease, so it is important to inhibit the activity of trypsin in the pancreas to ... One way in which the activity of trypsin is controlled is the production of a specific and potent trypsin inhibitor protein in ... This inhibitor binds tightly to trypsin, preventing the trypsin activity that would otherwise be detrimental to the organ. ... Although the trypsin inhibitor is a protein, it avoids being hydrolysed as a substrate by the protease by excluding water from ...
https://en.wikipedia.org/wiki/Enzyme_inhibitor
Albert J. R. HeckAlbert J. R. Heck
Tsiatsiani, Liana; Heck, Albert J. R. (2015). "Proteomics beyond trypsin". FEBS Journal. 282 (14): 2612-2626. doi:10.1111/febs. ... "Six alternative proteases for mass spectrometry-based proteomics beyond trypsin". Nature Protocols. 11 (5): 993-1006. doi: ...
https://en.wikipedia.org/wiki/Albert_J._R._Heck
Secretin-cholecystokinin testSecretin-cholecystokinin test
... trypsin, and lipase. These are measured by a catheter placed in the duodenum. Cholecystokinin also stimulates the flow of bile ...
https://en.wikipedia.org/wiki/Secretin-cholecystokinin_test
Ágústa GuðmundsdóttirÁgústa Guðmundsdóttir
... trypsin X isoenzymes (2017) Potential use of Atlantic cod trypsin in Biomedicine (2013). Gudmundsdóttir, Á., Stefánsson, B. and ... Zymetech makes use of trypsins from North-Atlantic Cod, which through the years has for the most part been discarded, and in ... Biochemical characterization of a native group III trypsin ZT from Atlantic cod (Gadus morhua) (2019) Elucidation of different ... Bjarnason, J. B. (2013). Trypsin I in Fish. In Neil D. Rawlings and Guy S. Salvesen, Handbook of Proteolytic Enzymes, 3rd ed. ( ...
https://en.wikipedia.org/wiki/Ágústa_Guðmundsdóttir
AprotininAprotinin
Kunitz M, Northrop JH (July 1936). "Isolation from beef pancreas of crystalline trypsinogen, trypsin, trypsin inhibitor, and an ... or basic trypsin inhibitor of bovine pancreas, which is an antifibrinolytic molecule that inhibits trypsin and related ... "Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at ... and independently as a trypsin inhibitor from bovine pancreas in 1936. It was purified from bovine lung in 1964. As it inhibits ...
https://en.wikipedia.org/wiki/Aprotinin
40S ribosomal protein S1540S ribosomal protein S15
A study with immobilized trypsin". FEBS Lett. 232 (2): 281-5. doi:10.1016/0014-5793(88)80753-1. PMID 3378620. S2CID 44333810. ...
https://en.wikipedia.org/wiki/40S_ribosomal_protein_S15
SPINK1SPINK1
Pancreatic secretory trypsin inhibitor (PSTI) also known as serine protease inhibitor Kazal-type 1 (SPINK1) or tumor-associated ... Tomita N, Horii A, Yamamoto T, Ogawa M, Mori T, Matsubara K (Dec 1987). "Expression of pancreatic secretory trypsin inhibitor ... PSTI serves to cleave prematurely activated trypsin to prevent the enzyme from causing cellular damage to the organ. Without ... Chen JM, Mercier B, Audrezet MP, Ferec C (Jan 2000). "Mutational analysis of the human pancreatic secretory trypsin inhibitor ( ...
https://en.wikipedia.org/wiki/SPINK1
Arthur W. ThomasArthur W. Thomas
Thomas, A. W., & Seymour-Jones, F. L. (1923). Hydrolysis of collagen by trypsin. Journal of the American Chemical Society, 45, ... Industrial and Engineering Chemistry, 16, 31-2. Thomas, A. W., & Seymour-Jones, F. L. (1924). Action of trypsin upon diverse ...
https://en.wikipedia.org/wiki/Arthur_W._Thomas
ProteaseProtease
This is the case for digestive enzymes such as trypsin, which have to be able to cleave the array of proteins ingested into ... For example, trypsin is specific for the sequences ...K\... or ...R\... ('\'=cleavage site). Conversely some proteases are ... Common examples are the trypsin inhibitors found in the seeds of some plants, most notable for humans being soybeans, a major ... ISBN 978-1-4160-2973-1. Rodriguez J, Gupta N, Smith RD, Pevzner PA (January 2008). "Does trypsin cut before proline?". Journal ...
https://en.wikipedia.org/wiki/Protease
40S ribosomal protein S2540S ribosomal protein S25
A study with immobilized trypsin". FEBS Letters. 232 (2): 281-5. doi:10.1016/0014-5793(88)80753-1. PMID 3378620. S2CID 44333810 ...
https://en.wikipedia.org/wiki/40S_ribosomal_protein_S25
TryptaseTryptase
"Mammalian tissue trypsin-like enzymes. Comparative reactivities of human skin tryptase, human lung tryptase, and bovine trypsin ... Kido H, Fukusen N, Katunuma N (June 1985). "Chymotrypsin- and trypsin-type serine proteases in rat mast cells: properties and ...
https://en.wikipedia.org/wiki/Tryptase
Endoproteinase Lys-CEndoproteinase Lys-C
Trypsin Lys-N Jekel, PA; Weijer, WJ; Beintema, JJ (15 October 1983). "Use of endoproteinase Lys-C from Lysobacter enzymogenes ...
https://en.wikipedia.org/wiki/Endoproteinase_Lys-C
Kunitz domainKunitz domain
... mammalian inter-alpha-trypsin inhibitors; trypstatin, a rat mast cell inhibitor of trypsin; a domain found in an alternatively ... Bovine pancreatic trypsin inhibitor is an extensively studied model structure. Certain family members are similar to the tick ... Wlodawer A, Housset D, Kim KS, Fuchs J, Woodward C (1991). "Crystal structure of a Y35G mutant of bovine pancreatic trypsin ... Takahashi K, Ikeo K, Gojobori T (1992). "Evolutionary origin of a Kunitz-type trypsin inhibitor domain inserted in the amyloid ...
https://en.wikipedia.org/wiki/Kunitz_domain
Funk Bros. Seed Co. v. Kalo Inoculant Co.Funk Bros. Seed Co. v. Kalo Inoculant Co.
In that case, the patentee desired to administer trypsin orally for use as an anti-inflammatory. He discovered that trypsin ... The patentee proposed and claimed coating trypsin with an enteric coating (stomach-acid-resistant coating), which permitted the ... any artisan would have known the process of enterically coating the trypsin to enable it to pass through the acidic environment ... Once nature's secret that the ileum would absorb trypsin was uncovered, ...
https://en.wikipedia.org/wiki/Funk_Bros._Seed_Co._v._Kalo_Inoculant_Co.
Bowman-Birk protease inhibitorBowman-Birk protease inhibitor
Trypsin- and chymotrypsin-inhibitor from soybeans". International Journal of Peptide and Protein Research. 25 (2): 113-31. doi: ... Tashiro M, Hashino K, Shiozaki M, Ibuki F, Maki Z (August 1987). "The complete amino acid sequence of rice bran trypsin ...
https://en.wikipedia.org/wiki/Bowman–Birk_protease_inhibitor
ITIH2ITIH2
"Analysis of inter-alpha-trypsin inhibitor and a novel trypsin inhibitor, pre-alpha-trypsin inhibitor, from human plasma. ... Inter-alpha-trypsin inhibitor heavy chain H2 is a protein that in humans is encoded by the ITIH2 gene. It is known to contain a ... Inter-alpha-trypsin inhibitor ITIH1 ITIH3 ITIH4 GRCh38: Ensembl release 89: ENSG00000151655 - Ensembl, May 2017 GRCm38: Ensembl ... 1988). "Isolation and characterization of cDNAs encoding the heavy chain of human inter-alpha-trypsin inhibitor (I alpha TI): ...
https://en.wikipedia.org/wiki/ITIH2
Peptidase inhibitor 15Peptidase inhibitor 15
This gene encodes a trypsin inhibitor. The protein shares similarity to insect venom allergens, mammalian testis-specific ...
https://en.wikipedia.org/wiki/Peptidase_inhibitor_15
TYSND1TYSND1
Trypsin domain containing 1 is a protein that in humans is encoded by the TYSND1 gene. This gene encodes a protease that ... "Entrez Gene: Trypsin domain containing 1". Retrieved 2017-10-02. Grupe A, Li Y, Rowland C, Nowotny P, Hinrichs AL, Smemo S, ...
https://en.wikipedia.org/wiki/TYSND1
TryptoneTryptone
"The Kinetics of Trypsin Digestion" (PDF). The Journal of Biological Chemistry. Retrieved 28 July 2014. "Indole Test". American ... Tryptone is the assortment of peptides formed by the digestion of casein by the protease trypsin. Tryptone is commonly used in ...
https://en.wikipedia.org/wiki/Tryptone
F2RL3F2RL3
Miike S, McWilliam AS, Kita H (2002). "Trypsin induces activation and inflammatory mediator release from human eosinophils ... F2RL3 is activated by thrombin and trypsin. Protease-activated receptor GRCh38: Ensembl release 89: ENSG00000127533 - Ensembl, ...
https://en.wikipedia.org/wiki/F2RL3
Venombin AVenombin A
Homology with the trypsin/kallikrein gene family". The Journal of Biological Chemistry. 263 (16): 7628-31. doi:10.1016/S0021- ...
https://en.wikipedia.org/wiki/Venombin_A
ChymotrypsinChymotrypsin
Trypsin PA clan of proteases PDB: 1CHG​; Freer ST, Kraut J, Robertus JD, Wright HT, Xuong NH (April 1970). "Chymotrypsinogen: ... Trypsin activates chymotrypsinogen by cleaving peptidic bonds in positions Arg15 - Ile16 and produces π-chymotrypsin. In turn, ... It is activated in the presence of trypsin. The hydrophobic and shape complementarity between the peptide substrate P1 side ...
https://en.wikipedia.org/wiki/Chymotrypsin
Phage monographsPhage monographs
The Chemistry of Pepsin, Trypsin, and Bacteriophage. Columbia University Press, New York. OCLC 2387455 d'Hérelle, F. 1938. Le ...
https://en.wikipedia.org/wiki/Phage_monographs
PRSS2PRSS2
Protease, serine, 2 (trypsin 2) is a protein that in humans is encoded by the PRSS2 gene. This gene encodes a trypsinogen, ... Baptista AM, Jonson PH, Hough E, Petersen SB (September 1998). "The origin of trypsin: evidence for multiple gene duplications ... "Entrez Gene: Protease, serine, 2 (trypsin 2)". Williams SJ, Gotley DC, Antalis TM (July 2001). "Human trypsinogen in colorectal ... which is a member of the trypsin family of serine proteases. This enzyme is secreted by the pancreas and cleaved to its active ...
https://en.wikipedia.org/wiki/PRSS2
Trypsin and chymotrypsin in stool: MedlinePlus Medical EncyclopediaTrypsin and chymotrypsin in stool: MedlinePlus Medical Encyclopedia
When the pancreas does not produce enough trypsin and chymotrypsin, smaller-than-normal amounts can be seen in ... Trypsin and chymotrypsin are substances released from the pancreas during normal digestion. ... Trypsin - plasma or serum. In: Chernecky CC, Berger BJ, eds. Laboratory Tests and Diagnostic Procedures. 6th ed. St Louis MO: ... Trypsin and chymotrypsin are substances released from the pancreas during normal digestion. When the pancreas does not produce ...
https://medlineplus.gov/ency/article/003594.htm
DailyMed - Search Results for Trypsin InhibitorsDailyMed - Search Results for Trypsin Inhibitors
Due to inconsistencies between the drug labels on DailyMed and the pill images provided by RxImage, we no longer display the RxImage pill images associated with drug labels. We anticipate reposting the images once we are able identify and filter out images that do not match the information provided in the drug labels. ...
https://dailymed.nlm.nih.gov/dailymed/search.cfm?query=Trypsin%20Inhibitors&searchdb=class
Serum trypsin inhibitor capacity and purulent sputumSerum trypsin inhibitor capacity and purulent sputum
... Am Rev Respir Dis. 1972 Nov;106(5):772-3. doi: 10.1164/arrd.1972.106.5.772 ...
https://pubmed.ncbi.nlm.nih.gov/5078876/
trypsin Clinical Research Trials | CenterWatchtrypsin Clinical Research Trials | CenterWatch
trypsin. Deficiency (AATD) is a genetic disease with lung and liver disease presentations. The purpose of this study is to ... trypsin. /EDTA to isolate epithelial cells from tissue, and uses murine 3T3 cells as feeder cells, which ... trypsin. deficiency (A1ATD). These novel MRI measures will be compared to matched contemporary clinical diagnostic tools, ... trypsin Clinical Research Trial Listings on CenterWatch ...
https://www.centerwatch.com/clinical-trials/listings/search/?q=trypsin
Trypsin Function: A Proteolytic Enzyme Vital for Good HealthTrypsin Function: A Proteolytic Enzyme Vital for Good Health
Trypsin is a digestive enzyme thats critical for good health. It helps break down dietary protein into amino acids, which are ... Trypsin and cancer. More research is being conducted on trypsin as it relates to cancer. While some research indicates trypsin ... Trypsin function. Trypsin is an enzyme that helps us digest protein. In the small intestine, trypsin breaks down proteins, ... 2006). The role of trypsin, trypsin inhibitor, and trypsin receptor in the onset and aggravation of pancreatitis [Abstract]. ...
https://www.healthline.com/health/trypsin-function
Trypsin (2014025) - DISCONTINUED | Rady Children's Hospital
ARUP 2014025 Trypsin test DISCONTINUED 10/3/2022 - Unable to locate test at another lab ...
https://www.rchsd.org/lab-test/trypsin-2014025/
Trypsin Neutralizer SolutionTrypsin Neutralizer Solution
A sterile, phosphate-buffered saline solution (1X) containing calf serum as a trypsin inhibitor. ... containing calf serum as a trypsin inhibitor. ...
https://www.thermofisher.com/order/catalog/product/R002100
Trypsin cleavage stabilizes the rotavirus VP4 spike - PubMedTrypsin cleavage stabilizes the rotavirus VP4 spike - PubMed
To examine the structural basis of trypsin-enhanced infectivity in rotaviruses, SA11 4F triple-layered particles (TLPs) grown ... in the absence (nontrypsinized rotavirus [NTR]) or presence (trypsinized rotavirus [TR]) of trypsin were chara … ... Trypsin enhances rotavirus infectivity by an unknown mechanism. ... Trypsin cleavage stabilizes the rotavirus VP4 spike S E ... Trypsin enhances rotavirus infectivity by an unknown mechanism. To examine the structural basis of trypsin-enhanced infectivity ...
https://pubmed.ncbi.nlm.nih.gov/11390607
SCOP 1.55: Superfamily b.47.1: Trypsin-like serine proteasesSCOP 1.55: Superfamily b.47.1: Trypsin-like serine proteases
More info for Superfamily b.47.1: Trypsin-like serine proteases. Timeline for Superfamily b.47.1: Trypsin-like serine proteases ... Superfamily b.47.1: Trypsin-like serine proteases appears in SCOP 1.57. *Superfamily b.47.1: Trypsin-like serine proteases ... Fold b.47: Trypsin-like serine proteases [50493] (1 superfamily). *. Superfamily b.47.1: Trypsin-like serine proteases [50494 ... Lineage for Superfamily b.47.1: Trypsin-like serine proteases. *Root: SCOP 1.55 *. Class b: All beta proteins [48724] (93 folds ...
http://scop.berkeley.edu/sunid=50494&ver=1.55
Performance comparison of three trypsin columns used in liquid chromatography - PubMedPerformance comparison of three trypsin columns used in liquid chromatography - PubMed
Trypsin is the most widely used enzyme in proteomic research due to its high specificity. Although the in-solution digestion is ... Performance comparison of three trypsin columns used in liquid chromatography Tereza Šlechtová 1 , Martin Gilar 2 , Květa ... Immobilization of trypsin on sub-micron skeletal polymer monolith. Yao C, Qi L, Hu W, Wang F, Yang G. Yao C, et al. Anal Chim ... Performance comparison of three trypsin columns used in liquid chromatography Tereza Šlechtová et al. J Chromatogr A. 2017. . ...
https://www.ncbi.nlm.nih.gov/pubmed/28215403
Human Trypsin Pan Specific (PRSS1/2/3) Biotinylated Antibody BAF3586: R&D SystemsHuman Trypsin Pan Specific (PRSS1/2/3) Biotinylated Antibody BAF3586: R&D Systems
View Human Trypsin Pan Specific (PRSS1/2/3) Biotinylated Antibody (BAF3586) datasheet. ... Trypsin-3 has limited activity on trypsin inhibitors, and thus regulates general trypsin activity. Trypsin-1, -2, and -3 are ... Mouse trypsin-1 shares 74% aa identity with the human trypsin consensus sequence. Trypsin-1 and -2 cleave peptide bonds ... Detects human Trypsin 1, human Trypsin 2 and human Trypsin 3 in Western blots. ...
https://www.rndsystems.com/products/human-trypsin-pan-specific-prss1-2-3-biotinylated-antibody_baf3586
Development and validation of an enzyme-linked immunosorbent assay for feline trypsin-like immunoreactivity in: American...Development and validation of an enzyme-linked immunosorbent assay for feline trypsin-like immunoreactivity in: American...
Sample Population-Purified feline cationic trypsin (fCT) and rabbit anti-fCT antiserum; blood samples from 63 healthy cats. ... Abstract Objective-To develop and validate an ELISA for quantitative analysis of feline trypsin-like immunoreactivity (fTLI). ... Sample Population-Purified feline cationic trypsin (fCT) and rabbit anti-fCT antiserum; blood samples from 63 healthy cats. ... Sample Population-Purified feline cationic trypsin (fCT) and rabbit anti-fCT antiserum; blood samples from 63 healthy cats. ...
https://avmajournals.avma.org/view/journals/ajvr/61/6/ajvr.2000.61.620.xml?rskey=rIDhu7&result=2
Salt effects on the amide hydrogen exchange of bovine pancreatic trypsin inhibitor<...Salt effects on the amide hydrogen exchange of bovine pancreatic trypsin inhibitor<...
Christoffersen M, Bolvig S, Tüchsen E. Salt effects on the amide hydrogen exchange of bovine pancreatic trypsin inhibitor. ... Salt effects on the amide hydrogen exchange of bovine pancreatic trypsin inhibitor. I: Biochemistry. 1996 ; Bind 35. s. 2309- ... Christoffersen, M., Bolvig, S., & Tüchsen, E. (1996). Salt effects on the amide hydrogen exchange of bovine pancreatic trypsin ... Christoffersen, M, Bolvig, S & Tüchsen, E 1996, Salt effects on the amide hydrogen exchange of bovine pancreatic trypsin ...
https://forskning.ruc.dk/da/publications/salt-effects-on-the-amide-hydrogen-exchange-of-bovine-pancreatic-
Mutations in the pancreatic secretory trypsin inhibitor gene (PSTI/SPINK1) rather than the cationic trypsinogen gene (PRSS1)...Mutations in the pancreatic secretory trypsin inhibitor gene (PSTI/SPINK1) rather than the cationic trypsinogen gene (PRSS1)...
Trypsin plays a central role in pancreatic exocrine physiology by acting as a trigger enzyme leading to activation of all other ... Intrapancreatic levels of trypsin are expected to be raised if mutations in the inhibitor molecule lead to loss of its ... Pancreatic secretory trypsin inhibitor (PSTI/SPINK1) is a potent protease inhibitor and thought to be a major protective ... The exact mechanism is still not clear and it remains to be proven how the prematurely activated trypsin is sustained inside ...
https://jmg.bmj.com/content/39/5/347
PDB-101: Molecule of the Month: TrypsinPDB-101: Molecule of the Month: Trypsin
An activated serine amino acid in trypsin cleaves protein chains ... Trypsinogen (left) and trypsin with trypsin inhibitor (red, ... An activated serine amino acid in trypsin cleaves protein chains Serine proteases: trypsin (top), chymotrypsin (center), and ... trypsin inhibitor (shown in red), that binds to any traces of active trypsin that might be present before it is secreted into ... Trypsin is built with an extra piece of protein chain, colored in green in the structure on the left (PDB entry 1tgs ). ...
https://pdb101.rcsb.org/motm/46
enQuireBio™ Recombinant Rat Anionic trypsin-1 Protein 100μg enQuireBio™ Recombinant Rat Anionic trypsin-1 Protein | Fisher...enQuireBio™ Recombinant Rat Anionic trypsin-1 Protein 100μg enQuireBio™ Recombinant Rat Anionic trypsin-1 Protein | Fisher...
Shop enQuireBio™ Recombinant Rat Anionic trypsin-1 Protein at Fishersci.dk ... A DNA sequence encoding the Rattus norvegicus (Rat) Anionic trypsin-1, was expressed in the hosts and tags indicated. ...
https://www.fishersci.dk/shop/products/recombinant-rat-anionic-trypsin-1-protein-6/16088141
KEGG entry for human inter-alpha-trypsin inhibitor heavy chain family, member 4 ITIH4KEGG entry for human inter-alpha-trypsin inhibitor heavy chain family, member 4 ITIH4
Publication: Semiempirical Comparative Binding Energy Analysis (SE-COMBINE) of a Series of Trypsin Inhibitors - QuantumBio Inc.Publication: Semiempirical Comparative Binding Energy Analysis (SE-COMBINE) of a Series of Trypsin Inhibitors - QuantumBio Inc.
Publication: Semiempirical Comparative Binding Energy Analysis (SE-COMBINE) of a Series of Trypsin Inhibitors. February 14, ... Publication: Semiempirical Comparative Binding Energy Analysis (SE-COMBINE) of a Series of Trypsin Inhibitors ... of SE-COMBINE was used as an investigation of the intermolecular interactions between 88 benzamidine inhibitors and trypsin and ...
https://www.quantumbioinc.com/10-1021-ct050284j/
Retrievals - ImmunohistochemistryRetrievals - Immunohistochemistry
Trypsin looses 75% of its reactivity within 30 minutes at 37ºC.. *Incubate the slides in the trypsin solution for 20 minutes at ... Prepare a trypsin solution by dissolving the appropriate amount of powder in 0.05M Tris-HCl • CaCl2 solution. Do not add the ... Trypsin. *Note: The user should validate the most optimal enzyme concentration and incubation time for their stain. We ... solution to the trypsin any earlier than 5 minutes prior to incubation. ...
https://www.niehs.nih.gov/research/resources/protocols/protocols-immuno/retrievals/index.cfm
DailyMed - Search Results for Trypsin InhibitorsDailyMed - Search Results for Trypsin Inhibitors
Due to inconsistencies between the drug labels on DailyMed and the pill images provided by RxImage, we no longer display the RxImage pill images associated with drug labels. We anticipate reposting the images once we are able identify and filter out images that do not match the information provided in the drug labels. ...
https://www.dailymed.nlm.nih.gov/dailymed/search.cfm?query=Trypsin%20Inhibitors&searchdb=class
trypsin - Metabolic Healingtrypsin - Metabolic Healing
By continuing to browse or by clicking "Continue" below, you agree to the storing of first- and third-party cookies on your device to enhance site navigation, analyze site usage, and assist in our marketing efforts. *Scroll down to dismiss notice.ContinuePrivacy policy ...
https://metabolichealing.com/tag/trypsin/
Cystic Fibrosis Imaging: Practice Essentials, Radiography, Computed TomographyCystic Fibrosis Imaging: Practice Essentials, Radiography, Computed Tomography
Immunoreactive trypsin test. Infants with CF have elevated blood levels of immunoreactive trypsin (IRT), which can be ...
https://emedicine.medscape.com/article/354931-overview
Porcine Trypsin Solution - RMBIOPorcine Trypsin Solution - RMBIO
Trypsin is also used for the re-suspension of cells during cell culture and in proteomics research. 0.25% concentration. ... Porcine trypsin is used to remove adherent cells from a culture surface. ... Porcine trypsin is used to remove adherent cells from a culture surface. Trypsin is also used for the re-suspension of cells ... Porcine Trypsin Solution. Our porcine trypsin liquid solution is manufactured from material sourced in the US ...
https://rmbio.com/collections/protein-fractions/products/porcine-trypsin-solution
Story of Discovery: Genetic Insights into Pancreatitis - NIDDKStory of Discovery: Genetic Insights into Pancreatitis - NIDDK
Advancements in identifying trypsin-related genetic factors, and other new genetic variants supported by NIDDK, may lead to ... In 2000, mutations in the pancreatic secretory trypsin inhibitory gene (PST1/SPINK1), which encodes a trypsin inhibitory ... Trypsin-related Genetic Factors. In 1996, scientists identified the first pancreatitis-related gene mutation in patients with a ... Normally, the body has a fail-safe mechanism whereby trypsin is programmed to self-destruct if prematurely activated while ...
https://www.niddk.nih.gov/news/archive/2014/discovery-genetic-insights-pancreatitis
Trypsin And Chymotrypsin - Jatan ExportsTrypsin And Chymotrypsin - Jatan Exports
Disclaimer - The content provided on this website is for general information and doesnt interpret any medical, commercial, or chemical information. Readers shouldnt interpret any information given here as medical advice or its substitute. The company and its affiliates take no responsibility for the reliance or use of any information given herein.. API/chemicals covered by patents are not offered to the countries where valid patent law is in force. However, the final responsibility lies with the customer.. ...
https://jatanexports.com/api/trypsin-and-chymotrypsin/
No.30713549] Sheffield Porcine Trypsin - ANHNo.30713549] Sheffield Porcine Trypsin - ANH
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https://www.anhsci.com/product/kerry/single-ingredient/sheffield-porcine-trypsin/no-30713549/
Effect of in vitro gastrointestinal digestion on the antibacterial activity of bioactive dairy formulas supplemented with...Effect of in vitro gastrointestinal digestion on the antibacterial activity of bioactive dairy formulas supplemented with...
Trypsin activity assay. This analysis, described by Brodkorb et al. (2019), was carried out to assess the activity of the ... For this, a solution of trypsin at different concentrations: 10 µg/mL, 15 µg/mL and 20 µg/mL in 1 mM HCl and 46 mM Tris-HCl ... The reaction of TAME in the presence of trypsin produces p-toluene-sulfonyl-l-arginine and methanol. The objective of the test ... First, 2.6 mL of Tris-HCl buffer was mixed with 300 µL of TAME and 100 µL of trypsin and then, continuous absorbance ...
https://link.springer.com/article/10.1007/s10534-022-00459-5
RCSB PDB Group Summary: 319 100RCSB PDB Group Summary: 319 100
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
https://www.rcsb.org/groups/summary/polymer_entity/319_100
TANNINS FROM DIFFERENT FOODSTUFFS AS TRYPSIN INHIBITORS. TANNINS FROM DIFFERENT FOODSTUFFS AS TRYPSIN INHIBITORS.
The trypsin inhibitory effect of phenolic extracts from different plant foodstuffs: two bean varieties, black and green tea and ... The trypsin inhibitory effect of phenolic extracts from different plant foodstuffs: two bean varieties, black and green tea and ... All of the plant phenolic extracts used in the experiments showed high level of the trypsin inhibition except for white bean ... The salting out of high molecular polyphenols reduced trypsin inhibiting effect of the examined extracts by 14-68%. ...
http://journal.pan.olsztyn.pl/TANNINS-FROM-DIFFERENT-FOODSTUFFS-AS-TRYPSIN-INHIBITORS-,97770,0,2.html
Trypsin, Bromelain, Rutoside Trihydrate & Diclofenac Sodium TabletsTrypsin, Bromelain, Rutoside Trihydrate & Diclofenac Sodium Tablets
... MANUFACTURERS SUPPLIERS - THIRD PARTY CONTRACT ...
https://www.krishlarpharma.com/product/kritheal-tablets/
InhibitorPancreasChymotrypsin in the stoolPancreatic secretory trypsinAmount of trypsinActive trypsinPorcine TrypsinProteaseProteinsAmylaseProteinCationicTrypsinogenEnzymeSerumProteolyticInhibitoryEnzymesProteasesGeneAnionicGeneticSequenceTabletsAcidActivityTissuePancreatitisAmountsMechanismTestHumanCellsOrganicSolutionLevelsHighRoleCommonShareStructureAdditional
Inhibitor4
  • 2006). The role of trypsin, trypsin inhibitor, and trypsin receptor in the onset and aggravation of pancreatitis [Abstract]. (healthline.com)
  • A sterile, phosphate-buffered saline solution (1X) containing calf serum as a trypsin inhibitor. (thermofisher.com)
  • Pancreatic secretory trypsin inhibitor (PSTI/SPINK1) is a potent protease inhibitor and thought to be a major protective mechanism preventing inappropriate activation of pancreatic digestive enzyme cascade by inhibiting up to 20% of potential trypsin activity. (bmj.com)
  • As extra insurance, the pancreas also makes a small protein, trypsin inhibitor (shown in red), that binds to any traces of active trypsin that might be present before it is secreted into the intestine. (rcsb.org)
Pancreas12
  • Trypsin and chymotrypsin are substances released from the pancreas during normal digestion. (medlineplus.gov)
  • When the pancreas does not produce enough trypsin and chymotrypsin, smaller-than-normal amounts can be seen in a stool sample. (medlineplus.gov)
  • Trypsin is produced by the pancreas in an inactive form called trypsinogen. (healthline.com)
  • If your pancreas doesn't produce enough trypsin, you can experience a digestive issue called malabsorption - the decreased ability to digest or absorb nutrients from food. (healthline.com)
  • Older research shows that production of trypsin in tissues other than the pancreas - tumor-derived trypsin - may be involved with the malignant growth of cancer cells. (healthline.com)
  • Most of these supplements combine trypsin - typically extracted from the pancreas of meat-producing animals - in various dosages with other enzymes. (healthline.com)
  • Trypsin in Greek means "rubbing or friction", and it was chosen here because the first trypsins were extracted from pancreas via a glycerin-based rubbing maceration. (rndsystems.com)
  • The pancreas adds a collection of protein-cutting enzymes, with trypsin playing the central role, that chop the protein chains into pieces just a few amino acids long. (rcsb.org)
  • Trypsinogen is produced by cells in the pancreas then secreted into the small intestine, where it becomes activated to trypsin, an enzyme that breaks down protein and activates other digestive enzymes. (nih.gov)
  • Normally, the body has a fail-safe mechanism whereby trypsin is programmed to self-destruct if prematurely activated while still inside the pancreas. (nih.gov)
  • However, the mutations in the trypsinogen gene found in patients with hereditary pancreatitis disable this mechanism, enhancing trypsin activation in the pancreas, where it causes cell damage and pancreatitis. (nih.gov)
  • TPCK Treated Trypsin is purified from Bovine Pancreas. (proteochem.com)
Chymotrypsin in the stool2
  • The result is normal if there is a normal amount of trypsin or chymotrypsin in the stool. (medlineplus.gov)
  • In adults, low amounts of trypsin and chymotrypsin in the stool are an indicator of cystic fibrosis and pancreatic diseases, such as pancreatitis. (healthline.com)
Pancreatic secretory trypsin1
  • In 2000, mutations in the pancreatic secretory trypsin inhibitory gene (PST1/SPINK1), which encodes a trypsin inhibitory protein, were identified in patients with pancreatitis that cause a loss of this inhibitory function, disabling this first line of defense against prematurely activated trypsin in the pancreas. (nih.gov)
Amount of trypsin1
  • Measuring the amount of trypsin in your body can help identify healthy problems such as pancreatitis and cystic fibrosis. (healthline.com)
Active trypsin2
  • The trypsinogen enters the small intestine through the common bile duct and is converted to active trypsin. (healthline.com)
  • This active trypsin acts with the other two principal digestive proteinases - pepsin and chymotrypsin - to break down dietary protein into peptides and amino acids. (healthline.com)
Porcine Trypsin1
  • Porcine trypsin is used to remove adherent cells from a culture surface. (rmbio.com)
Protease5
  • Trypsin uses a special serine amino acid in its protein-cutting reaction, and is consequently known as a serine protease. (rcsb.org)
  • Trypsin protease cleaves peptide bonds with selectivity for Arg and Lys residues. (proteochem.com)
  • Optimum trypsin protease activity is achieved at pH 8.0 to 9.0. (proteochem.com)
  • ProteoChem s trypsin protease is supplied as a lyophilized powder with minimum activity of 180 units per mg. (proteochem.com)
  • Mass spectrometry and amino-terminal sequence analysis identified the purified protease as chicken trypsin II P29. (cdc.gov)
Proteins3
  • In the small intestine, trypsin breaks down proteins, continuing the process of digestion that began in the stomach. (healthline.com)
  • In digestion, trypsin, chymotrypsin and elastase work together to chop up proteins. (rcsb.org)
  • Later, additional genes coding for proteins that affect trypsin activation, such as the chymotrypsinogen C gene and calcium sensing receptor gene, were also found to contribute to pancreatitis susceptibility. (nih.gov)
Amylase1
  • What is common among amylase, renin and trypsin? (gneet.com)
Protein6
  • Trypsin is an enzyme that helps us digest protein. (healthline.com)
  • Trypsin is an enzyme that is essential for your body to digest protein, a critical component for building and repairing tissue including bones, muscles, cartilage, skin, and blood. (healthline.com)
  • 1999). Expression of trypsin in human cancer cell lines and cancer tissues and its tight binding to soluble form of Alzheimer amyloid precursor protein in culture [Abstract]. (healthline.com)
  • To examine the structural basis of trypsin-enhanced infectivity in rotaviruses, SA11 4F triple-layered particles (TLPs) grown in the absence (nontrypsinized rotavirus [NTR]) or presence (trypsinized rotavirus [TR]) of trypsin were characterized to determine the structure, the protein composition, and the infectivity of the particles before and after trypsin treatment. (nih.gov)
  • This longer form of trypsin, called trypsinogen, is inactive and cannot cut protein chains. (rcsb.org)
  • This gene coded for the protein cationic trypsinogen, an inactive precursor form of the digestive enzyme trypsin. (nih.gov)
Cationic1
  • Trypsin-1 (cationic), -2 (anionic), and -3 (mesotrypsin) are synthesized as 26 kDa trypsinogens (plus a 35 kDa trypsinogen-3 isoform) that are 247 amino acids (aa) in length. (rndsystems.com)
Trypsinogen1
  • Since that initial groundbreaking discovery, additional mutations associated with pancreatitis were identified in the trypsinogen gene, as well as in other genes that relate to trypsinogen/trypsin function. (nih.gov)
Enzyme3
  • One study concludes that the combination of trypsin and chymotrypsin is more effective in addressing inflammatory symptoms and recovery of severe tissue injury than many other enzyme preparations. (healthline.com)
  • Trypsin is the most widely used enzyme in proteomic research due to its high specificity. (nih.gov)
  • Then, when it enters the intestine, the enzyme enteropeptidase makes one cut in the trypsin chain, clipping off the little tail. (rcsb.org)
Serum1
Proteolytic1
  • To overcome these shortcomings trypsin was covalently immobilized on solid support and tested for its proteolytic activity. (nih.gov)
Inhibitory1
  • The trypsin inhibitory effect of phenolic extracts from different plant foodstuffs: two bean varieties, black and green tea and quince fruits as well as of standard phenolic compounds: (+)catechin, (-)epicatechin, gallic acid and tannic acid, was investigated. (olsztyn.pl)
Enzymes2
  • Trypsin is a general term for any of three 24 kDa gene products that belong to the peptidase S1 family of enzymes. (rndsystems.com)
  • Trypsin-like enzymes are also found in many other places in the body. (rcsb.org)
Proteases1
  • Serine proteases: trypsin (top), chymotrypsin (center), and elastase (bottom). (rcsb.org)
Gene1
  • Characterisation and expression of the late trypsin gene in Aedes aegypti / by Frederick Obonyo Oduol. (who.int)
Anionic1
  • A DNA sequence encoding the Rattus norvegicus (Rat) Anionic trypsin-1, was expressed in the hosts and tags indicated. (fishersci.dk)
Genetic1
  • Alpha-1 Anti- trypsin Deficiency (AATD) is a genetic disease with lung and liver disease presentations. (centerwatch.com)
Sequence1
  • Mouse trypsin-1 shares 74% aa identity with the human trypsin consensus sequence. (rndsystems.com)
Tablets1
  • Prominent & Leading Exporter from Palghar, we offer chysin (trypsin chymotrypsin), dexamethasone tablets, dexamethasone tablet,dekot tablets 0.5mg, carbin-5 (carbimazole) and piroxicam capsules bp 40mg. (tabletandcapsules.com)
Acid2
  • Monomeric tannin precursors exhibited 1000-times lower activity in the trypsin inhibition than high-molecular tannic acid. (olsztyn.pl)
  • Did you mean trypsin BLUE FREE ACID ? (nih.gov)
Activity2
  • Trypsin-3 has limited activity on trypsin inhibitors, and thus regulates general trypsin activity. (rndsystems.com)
  • Our trypsin is chromatographically purified, diafiltered, and TPCK treated to remove chymotryptic activity. (proteochem.com)
Tissue1
  • There are people who advocate using trypsin for direct application to wounds - including mouth ulcers - suggesting that it removes dead tissue and promotes healthy tissue growth. (healthline.com)
Pancreatitis1
  • Doctors will check the level of trypsin in your blood as a test to diagnose pancreatitis . (healthline.com)
Amounts1
  • Doctors also check for the of amounts of trypsin and chymotrypsin that appear in the blood and stool. (healthline.com)
Mechanism1
  • Trypsin enhances rotavirus infectivity by an unknown mechanism. (nih.gov)
Test2
  • This article discusses the test to measure trypsin and chymotrypsin in stool. (medlineplus.gov)
  • The application of SE-COMBINE was used as an investigation of the intermolecular interactions between 88 benzamidine inhibitors and trypsin and to test the ability of this new method to predict binding free energies. (quantumbioinc.com)
Human1
  • Detects human Trypsin 1, human Trypsin 2 and human Trypsin 3 in Western blots. (rndsystems.com)
Cells1
  • Trypsin is also used for the re-suspension of cells during cell culture and in proteomics research. (rmbio.com)
Organic1
  • Our studies have shown that chicken trypsin is a proinflammatory constituent of poultry organic dust, and induces lung inflammatory mediators via increased ROS and PAR activation in a cell signaling pathway involving PKC, MAPK1/3 and MAPK14 and NF-kB and Stat-3. (cdc.gov)
Solution1
  • Dissociate the cel s that have become confluent in the culture flask using trypsin-EDTA solution with or without the use of a cell scraper and subculture in a culture flask or inoculate into 96-wel plates. (nih.gov)
Levels1
  • An abnormal result means the trypsin or chymotrypsin levels in your stool are below the normal range. (medlineplus.gov)
High1
  • All of the plant phenolic extracts used in the experiments showed high level of the trypsin inhibition except for white bean one. (olsztyn.pl)
Role2
  • While some research indicates trypsin may have a tumor-suppressive role in cancer progression, other research shows that trypsin promotes proliferation, invasion, and metastasis in various cancers. (healthline.com)
  • There is ongoing study to determine the role of trypsin in regard to supporting or attacking cancerous tumors. (healthline.com)
Common1
  • 1, 2 Although the exact pathogenesis is not clear, autodigestion secondary to aberrant intraductal activation of zymogens by trypsin is a primary common event. (bmj.com)
Share1
  • Over their mature regions, the three trypsins share 84% aa identity. (rndsystems.com)
Structure1
  • Structural studies on the NTR TLPs after trypsin treatment showed that spike structure could be partially recovered. (nih.gov)
Additional1
  • Following additional trypsin treatment, infectivity was enhanced for both NTR and TR particles, but the infectivity of NTR remained 2 logs lower than that of TR particles. (nih.gov)