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.
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).
A high-molecular-weight protein (approximately 22,500) containing 198 amino acid residues. It is a strong inhibitor of trypsin and human plasmin.
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.
A low-molecular-weight protein (minimum molecular weight 8000) which has the ability to inhibit trypsin as well as chymotrypsin at independent binding sites. It is characterized by a high cystine content and the absence of glycine.
A 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)
The inactive proenzyme of trypsin secreted by the pancreas, activated in the duodenum via cleavage by enteropeptidase. (Stedman, 25th ed)
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.
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.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The sum of the weight of all the atoms in a molecule.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
The rate dynamics in chemical or physical systems.
A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
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.
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Amidines substituted with a benzene group. Benzamidine and its derivatives are known as peptidase inhibitors.
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.
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).
The process of cleaving a chemical compound by the addition of a molecule of water.
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 on non-ionic gels without regard to the mechanism of solute discrimination.
A proteolytic enzyme obtained from Streptomyces griseus.
A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.
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)
Glycoproteins with a molecular weight of approximately 620,000 to 680,000. Precipitation by electrophoresis is in the alpha region. They include alpha 1-macroglobulins and alpha 2-macroglobulins. These proteins exhibit trypsin-, chymotrypsin-, thrombin-, and plasmin-binding activity and function as hormonal transporters.
A 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 (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.
A heterogeneous mixture of glycoproteins responsible for the gel structure of egg white. It has trypsin-inhibiting activity.
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.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.
A 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.
An actinomycete from which the antibiotics STREPTOMYCIN, grisein, and CANDICIDIN are obtained.
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.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
The fluid containing digestive enzymes secreted by the pancreas in response to food in the duodenum.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
A group of amylolytic enzymes that cleave starch, glycogen, and related alpha-1,4-glucans. (Stedman, 25th ed) EC 3.2.1.-.
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).
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.
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 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.
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.
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
Physiologically inactive substances that can be converted to active enzymes.
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
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.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
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).
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
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.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Chymotrypsinogen is a zymogen, specifically an inactive precursor form of the enzyme chymotrypsin, which is produced in the pancreas and activated in the small intestine to help digest proteins by cleaving specific peptide bonds.
Fluids originating from the epithelial lining of the intestines, adjoining exocrine glands and from organs such as the liver, which empty into the cavity of the intestines.
A 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)
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.
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.
An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN.
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.
An annual legume. The SEEDS of this plant are edible and used to produce a variety of SOY FOODS.
Proteins prepared by recombinant DNA technology.
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.
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.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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.
Peptides composed of between two and twelve amino acids.
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.
A trypsin-like enzyme of spermatozoa which is not inhibited by alpha 1 antitrypsin.
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.
Established cell cultures that have the potential to propagate indefinitely.
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.
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.
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.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
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.
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)

Trypsin is a proteolytic enzyme, specifically a serine protease, that is secreted by the pancreas as an inactive precursor, trypsinogen. Trypsinogen is converted into its active form, trypsin, in the small intestine by enterokinase, which is produced by the intestinal mucosa.

Trypsin plays a crucial role in digestion by cleaving proteins into smaller peptides at specific arginine and lysine residues. This enzyme helps to break down dietary proteins into amino acids, allowing for their absorption and utilization by the body. Additionally, trypsin can activate other zymogenic pancreatic enzymes, such as chymotrypsinogen and procarboxypeptidases, thereby contributing to overall protein digestion.

Trypsin Inhibitor, Kazal Pancreatic is a type of protein that is produced in the pancreas and functions as an inhibitor to trypsin, which is a proteolytic enzyme involved in digestion. Specifically, this inhibitor belongs to the Kazal-type serine protease inhibitors. It helps regulate the activity of trypsin within the pancreas, preventing premature activation and potential damage to pancreatic tissue. Any imbalance or deficiency in this inhibitor can lead to pancreatic diseases such as pancreatitis.

Trypsin inhibitor, Kunitz soybean, also known as Bowman-Birk inhibitor, is a type of protease inhibitor found in soybeans. It is a small protein molecule that inhibits the activity of trypsin, a digestive enzyme that helps break down proteins in the body. The Kunitz soybean trypsin inhibitor has two binding sites for trypsin and is resistant to digestion, making it biologically active in the gastrointestinal tract. It can inhibit the absorption of trypsin and regulate its activity, which may have implications for protein digestion and the regulation of certain physiological processes.

Chymotrypsin is a proteolytic enzyme, specifically a serine protease, that is produced in the pancreas and secreted into the small intestine as an inactive precursor called chymotrypsinogen. Once activated, chymotrypsin helps to digest proteins in food by breaking down specific peptide bonds in protein molecules. Its activity is based on the recognition of large hydrophobic side chains in amino acids like phenylalanine, tryptophan, and tyrosine. Chymotrypsin plays a crucial role in maintaining normal digestion and absorption processes in the human body.

The Trypsin Inhibitor, Bowman-Birk Soybean is a type of protease inhibitor that is found in soybeans. It is named after its discoverer, Henry B. Bowman, and the location where it was first discovered, the Birk farm in Ohio. This protein inhibits the activity of trypsin, an enzyme that helps digest proteins in the body.

The Bowman-Birk Trypsin Inhibitor (BBTI) is a small protein with a molecular weight of approximately 8000 Da and consists of two inhibitory domains, each containing a reactive site for trypsin. This dual inhibitory property allows BBTI to inhibit both trypsin and chymotrypsin, another proteolytic enzyme.

BBTI has been studied extensively due to its potential health benefits. It has been shown to have anti-cancer properties, as it can inhibit the growth of cancer cells and induce apoptosis (programmed cell death). Additionally, BBTI may also have anti-inflammatory effects and has been shown to protect against oxidative stress.

However, it is important to note that excessive consumption of BBTI may interfere with protein digestion and absorption in the body, as it inhibits trypsin activity. Therefore, soybeans and soybean-derived products should be consumed in moderation as part of a balanced diet.

Aprotinin is a medication that belongs to a class of drugs called serine protease inhibitors. It works by inhibiting the activity of certain enzymes in the body that can cause tissue damage and bleeding. Aprotinin is used in medical procedures such as heart bypass surgery to reduce blood loss and the need for blood transfusions. It is administered intravenously and its use is typically stopped a few days after the surgical procedure.

Aprotinin was first approved for use in the United States in 1993, but its use has been restricted or withdrawn in many countries due to concerns about its safety. In 2006, a study found an increased risk of kidney damage and death associated with the use of aprotinin during heart bypass surgery, leading to its withdrawal from the market in Europe and Canada. However, it is still available for use in the United States under a restricted access program.

It's important to note that the use of aprotinin should be carefully considered and discussed with the healthcare provider, taking into account the potential benefits and risks of the medication.

Trypsinogen is a precursor protein that is converted into the enzyme trypsin in the small intestine. It is produced by the pancreas and released into the duodenum, where it is activated by enterokinase, an enzyme produced by the intestinal mucosa. Trypsinogen plays a crucial role in digestion by helping to break down proteins into smaller peptides and individual amino acids.

In medical terms, an elevated level of trypsinogen in the blood may indicate pancreatic disease or injury, such as pancreatitis or pancreatic cancer. Therefore, measuring trypsinogen levels in the blood is sometimes used as a diagnostic tool to help identify these conditions.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Proteinase-activated receptor 2 (PAR-2) is a type of G protein-coupled receptor that is widely expressed in various tissues, including the respiratory and gastrointestinal tracts, skin, and nervous system. PAR-2 can be activated by serine proteases such as trypsin, mast cell tryptase, and thrombin, which cleave the N-terminal extracellular domain of the receptor to expose a tethered ligand that binds to and activates the receptor.

Once activated, PAR-2 signaling can lead to a variety of cellular responses, including inflammation, pain, and altered ion channel activity. PAR-2 has been implicated in several physiological and pathophysiological processes, such as airway hyperresponsiveness, asthma, cough, gastrointestinal motility disorders, and skin disorders.

In summary, PAR-2 is a type of receptor that can be activated by serine proteases, leading to various cellular responses and involvement in several disease processes.

A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.

Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Peptide hydrolases, also known as proteases or peptidases, are a group of enzymes that catalyze the hydrolysis of peptide bonds in proteins and peptides. They play a crucial role in various biological processes such as protein degradation, digestion, cell signaling, and regulation of various physiological functions. Based on their catalytic mechanism and the specificity for the peptide bond, they are classified into several types, including serine proteases, cysteine proteases, aspartic proteases, and metalloproteases. These enzymes have important clinical applications in the diagnosis and treatment of various diseases, such as cancer, viral infections, and inflammatory disorders.

Protease inhibitors are a class of antiviral drugs that are used to treat infections caused by retroviruses, such as the human immunodeficiency virus (HIV), which is responsible for causing AIDS. These drugs work by blocking the activity of protease enzymes, which are necessary for the replication and multiplication of the virus within infected cells.

Protease enzymes play a crucial role in the life cycle of retroviruses by cleaving viral polyproteins into functional units that are required for the assembly of new viral particles. By inhibiting the activity of these enzymes, protease inhibitors prevent the virus from replicating and spreading to other cells, thereby slowing down the progression of the infection.

Protease inhibitors are often used in combination with other antiretroviral drugs as part of highly active antiretroviral therapy (HAART) for the treatment of HIV/AIDS. Common examples of protease inhibitors include saquinavir, ritonavir, indinavir, and atazanavir. While these drugs have been successful in improving the outcomes of people living with HIV/AIDS, they can also cause side effects such as nausea, diarrhea, headaches, and lipodystrophy (changes in body fat distribution).

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

The pancreas is a glandular organ located in the abdomen, posterior to the stomach. It has both exocrine and endocrine functions. The exocrine portion of the pancreas consists of acinar cells that produce and secrete digestive enzymes into the duodenum via the pancreatic duct. These enzymes help in the breakdown of proteins, carbohydrates, and fats in food.

The endocrine portion of the pancreas consists of clusters of cells called islets of Langerhans, which include alpha, beta, delta, and F cells. These cells produce and secrete hormones directly into the bloodstream, including insulin, glucagon, somatostatin, and pancreatic polypeptide. Insulin and glucagon are critical regulators of blood sugar levels, with insulin promoting glucose uptake and storage in tissues and glucagon stimulating glycogenolysis and gluconeogenesis to raise blood glucose when it is low.

Endopeptidases are a type of enzyme that breaks down proteins by cleaving peptide bonds inside the polypeptide chain. They are also known as proteinases or endoproteinases. These enzymes work within the interior of the protein molecule, cutting it at specific points along its length, as opposed to exopeptidases, which remove individual amino acids from the ends of the protein chain.

Endopeptidases play a crucial role in various biological processes, such as digestion, blood coagulation, and programmed cell death (apoptosis). They are classified based on their catalytic mechanism and the structure of their active site. Some examples of endopeptidase families include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.

It is important to note that while endopeptidases are essential for normal physiological functions, they can also contribute to disease processes when their activity is unregulated or misdirected. For instance, excessive endopeptidase activity has been implicated in the pathogenesis of neurodegenerative disorders, cancer, and inflammatory conditions.

Benzoylarginine nitroanilide is a synthetic peptide derivative that is often used as a substrate in enzyme assays, particularly for testing the activity of proteases (enzymes that break down proteins). Proteases cleave the peptide bond between benzoyl and arginine in the molecule, releasing p-nitroaniline, which can be easily measured spectrophotometrically. This allows researchers to quantify the activity of protease enzymes in a sample. It is also known as Benzoyl-L-arginine ρ-nitroanilide hydrochloride or BAPNA.

Serine proteinase inhibitors, also known as serine protease inhibitors or serpins, are a group of proteins that inhibit serine proteases, which are enzymes that cut other proteins in a process called proteolysis. Serine proteinases are important in many biological processes such as blood coagulation, fibrinolysis, inflammation and cell death. The inhibition of these enzymes by serpin proteins is an essential regulatory mechanism to maintain the balance and prevent uncontrolled proteolytic activity that can lead to diseases.

Serpins work by forming a covalent complex with their target serine proteinases, irreversibly inactivating them. The active site of serpins contains a reactive center loop (RCL) that mimics the protease's target protein sequence and acts as a bait for the enzyme. When the protease cleaves the RCL, it gets trapped within the serpin structure, leading to its inactivation.

Serpin proteinase inhibitors play crucial roles in various physiological processes, including:

1. Blood coagulation and fibrinolysis regulation: Serpins such as antithrombin, heparin cofactor II, and protease nexin-2 control the activity of enzymes involved in blood clotting and dissolution to prevent excessive or insufficient clot formation.
2. Inflammation modulation: Serpins like α1-antitrypsin, α2-macroglobulin, and C1 inhibitor regulate the activity of proteases released during inflammation, protecting tissues from damage.
3. Cell death regulation: Some serpins, such as PI-9/SERPINB9, control apoptosis (programmed cell death) by inhibiting granzyme B, a protease involved in this process.
4. Embryonic development and tissue remodeling: Serpins like plasminogen activator inhibitor-1 (PAI-1) and PAI-2 regulate the activity of enzymes involved in extracellular matrix degradation during embryonic development and tissue remodeling.
5. Neuroprotection: Serpins such as neuroserpin protect neurons from damage by inhibiting proteases released during neuroinflammation or neurodegenerative diseases.

Dysregulation of serpins has been implicated in various pathological conditions, including thrombosis, emphysema, Alzheimer's disease, and cancer. Understanding the roles of serpins in these processes may provide insights into potential therapeutic strategies for treating these diseases.

Serine endopeptidases are a type of enzymes that cleave peptide bonds within proteins (endopeptidases) and utilize serine as the nucleophilic amino acid in their active site for catalysis. These enzymes play crucial roles in various biological processes, including digestion, blood coagulation, and programmed cell death (apoptosis). Examples of serine endopeptidases include trypsin, chymotrypsin, thrombin, and elastase.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Benzamidines are a group of organic compounds that contain a benzene ring linked to an amidine functional group. They are commonly used as antimicrobial agents, particularly in the treatment of various gram-negative bacterial infections. Benzamidines work by inhibiting the enzyme bacterial dehydrogenases, which are essential for the bacteria's survival.

Some examples of benzamidine derivatives include:

* Tempanamine hydrochloride (Tembaglanil): used to treat urinary tract infections caused by susceptible strains of Escherichia coli and Klebsiella pneumoniae.
* Chlorhexidine: a broad-spectrum antimicrobial agent used as a disinfectant and preservative in various medical and dental applications.
* Prothiobenzamide: an anti-inflammatory and analgesic drug used to treat gout and rheumatoid arthritis.

It is important to note that benzamidines have a narrow therapeutic index, which means that the difference between an effective dose and a toxic dose is small. Therefore, they should be used with caution and under the supervision of a healthcare professional.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

Pancreatic elastase is a type of elastase that is specifically produced by the pancreas. It is an enzyme that helps in digesting proteins found in the food we eat. Pancreatic elastase breaks down elastin, a protein that provides elasticity to tissues and organs in the body.

In clinical practice, pancreatic elastase is often measured in stool samples as a diagnostic tool to assess exocrine pancreatic function. Low levels of pancreatic elastase in stool may indicate malabsorption or exocrine pancreatic insufficiency, which can be caused by various conditions such as chronic pancreatitis, cystic fibrosis, or pancreatic cancer.

Gel chromatography is a type of liquid chromatography that separates molecules based on their size or molecular weight. It uses a stationary phase that consists of a gel matrix made up of cross-linked polymers, such as dextran, agarose, or polyacrylamide. The gel matrix contains pores of various sizes, which allow smaller molecules to penetrate deeper into the matrix while larger molecules are excluded.

In gel chromatography, a mixture of molecules is loaded onto the top of the gel column and eluted with a solvent that moves down the column by gravity or pressure. As the sample components move down the column, they interact with the gel matrix and get separated based on their size. Smaller molecules can enter the pores of the gel and take longer to elute, while larger molecules are excluded from the pores and elute more quickly.

Gel chromatography is commonly used to separate and purify proteins, nucleic acids, and other biomolecules based on their size and molecular weight. It is also used in the analysis of polymers, colloids, and other materials with a wide range of applications in chemistry, biology, and medicine.

Pronase is not a medical term itself, but it is a proteolytic enzyme mixture derived from the bacterium Streptomyces griseus. The term "pronase" refers to a group of enzymes that can break down proteins into smaller peptides and individual amino acids by hydrolyzing their peptide bonds.

Pronase is used in various laboratory applications, including protein degradation, DNA and RNA isolation, and the removal of contaminating proteins from nucleic acid samples. It has also been used in some medical research contexts to study protein function and structure, as well as in certain therapeutic settings for its ability to break down proteins.

It is important to note that pronase is not a drug or a medical treatment itself but rather a laboratory reagent with potential applications in medical research and diagnostics.

Thermolysin is not a medical term per se, but it is a bacterial enzyme that is often used in biochemistry and molecular biology research. Here's the scientific or biochemical definition:

Thermolysin is a zinc metalloprotease enzyme produced by the bacteria Geobacillus stearothermophilus. It has an optimum temperature for activity at around 65°C, and it can remain active in high temperatures, which makes it useful in various industrial applications. Thermolysin is known for its ability to cleave peptide bonds, particularly those involving hydrophobic residues, making it a valuable tool in protein research and engineering.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Alpha-macroglobulins are a type of large protein molecule found in blood plasma, which play a crucial role in the human body's immune system. They are called "macro" globulins because of their large size, and "alpha" refers to their electrophoretic mobility, which is a laboratory technique used to separate proteins based on their electrical charge.

Alpha-macroglobulins function as protease inhibitors, which means they help regulate the activity of enzymes called proteases that can break down other proteins in the body. By inhibiting these proteases, alpha-macroglobulins help protect tissues and organs from excessive protein degradation and also help maintain the balance of various biological processes.

One of the most well-known alpha-macroglobulins is alpha-1-antitrypsin, which helps protect the lungs from damage caused by inflammation and protease activity. Deficiencies in this protein have been linked to lung diseases such as emphysema and chronic obstructive pulmonary disease (COPD).

Overall, alpha-macroglobulins are an essential component of the human immune system and play a critical role in maintaining homeostasis and preventing excessive tissue damage.

Papain is defined as a proteolytic enzyme that is derived from the latex of the papaya tree (Carica papaya). It has the ability to break down other proteins into smaller peptides or individual amino acids. Papain is widely used in various industries, including the food industry for tenderizing meat and brewing beer, as well as in the medical field for its digestive and anti-inflammatory properties.

In medicine, papain is sometimes used topically to help heal burns, wounds, and skin ulcers. It can also be taken orally to treat indigestion, parasitic infections, and other gastrointestinal disorders. However, its use as a medical treatment is not widely accepted and more research is needed to establish its safety and efficacy.

Cyanogen bromide is a solid compound with the chemical formula (CN)Br. It is a highly reactive and toxic substance that is used in research and industrial settings for various purposes, such as the production of certain types of resins and gels. Cyanogen bromide is an alkyl halide, which means it contains a bromine atom bonded to a carbon atom that is also bonded to a cyano group (a nitrogen atom bonded to a carbon atom with a triple bond).

Cyanogen bromide is classified as a class B poison, which means it can cause harm or death if swallowed, inhaled, or absorbed through the skin. It can cause irritation and burns to the eyes, skin, and respiratory tract, and prolonged exposure can lead to more serious health effects, such as damage to the nervous system and kidneys. Therefore, it is important to handle cyanogen bromide with care and to use appropriate safety precautions when working with it.

Ovomucin is a glycoprotein found in the egg white (albumen) of birds. It is one of the major proteins in egg white, making up about 10-15% of its total protein content. Ovomucin is known for its ability to form a gel-like structure when egg whites are beaten, which helps to protect the developing embryo inside the egg.

Ovomucin has several unique properties that make it medically interesting. For example, it has been shown to have antibacterial and antiviral activities, and may help to prevent microbial growth in the egg. Additionally, ovomucin is a complex mixture of proteins with varying molecular weights and structures, which makes it a subject of interest for researchers studying protein structure and function.

In recent years, there has been some research into the potential medical uses of ovomucin, including its possible role in wound healing and as a potential treatment for respiratory infections. However, more research is needed to fully understand the potential therapeutic applications of this interesting protein.

Pepsin A is defined as a digestive enzyme that is primarily secreted by the chief cells in the stomach's fundic glands. It plays a crucial role in protein catabolism, helping to break down food proteins into smaller peptides during the digestive process. Pepsin A has an optimal pH range of 1.5-2.5 for its enzymatic activity and is activated from its inactive precursor, pepsinogen, upon exposure to acidic conditions in the stomach.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

Peptide mapping is a technique used in proteomics and analytical chemistry to analyze and identify the sequence and structure of peptides or proteins. This method involves breaking down a protein into smaller peptide fragments using enzymatic or chemical digestion, followed by separation and identification of these fragments through various analytical techniques such as liquid chromatography (LC) and mass spectrometry (MS).

The resulting peptide map serves as a "fingerprint" of the protein, providing information about its sequence, modifications, and structure. Peptide mapping can be used for a variety of applications, including protein identification, characterization of post-translational modifications, and monitoring of protein degradation or cleavage.

In summary, peptide mapping is a powerful tool in proteomics that enables the analysis and identification of proteins and their modifications at the peptide level.

Thrombin receptors are a type of G protein-coupled receptor (GPCR) that play a crucial role in hemostasis and thrombosis. They are activated by the protease thrombin, which is generated during the coagulation cascade. There are two main types of thrombin receptors: protease-activated receptor 1 (PAR-1) and PAR-4.

PAR-1 is expressed on various cell types including platelets, endothelial cells, and smooth muscle cells, while PAR-4 is primarily expressed on platelets. Activation of these receptors triggers a variety of intracellular signaling pathways that lead to diverse cellular responses such as platelet activation, aggregation, and secretion; vasoconstriction; and inflammation.

Dysregulation of thrombin receptor signaling has been implicated in several pathological conditions, including arterial and venous thrombosis, atherosclerosis, and cancer. Therefore, thrombin receptors are considered important therapeutic targets for the treatment of these disorders.

"Streptomyces griseus" is a species of bacteria that belongs to the family Streptomycetaceae. This gram-positive, aerobic, and saprophytic bacterium is known for its ability to produce several important antibiotics, including streptomycin, grisein, and candidin. The bacterium forms a branched mycelium and is commonly found in soil and aquatic environments. It has been widely studied for its industrial applications, particularly in the production of antibiotics and enzymes.

The medical significance of "Streptomyces griseus" lies primarily in its ability to produce streptomycin, a broad-spectrum antibiotic that is effective against many gram-positive and gram-negative bacteria, as well as some mycobacteria. Streptomycin was the first antibiotic discovered to be effective against tuberculosis and has been used in the treatment of this disease for several decades. However, due to the emergence of drug-resistant strains of Mycobacterium tuberculosis, streptomycin is now rarely used as a first-line therapy for tuberculosis but may still be used in combination with other antibiotics for the treatment of multidrug-resistant tuberculosis.

In addition to its role in antibiotic production, "Streptomyces griseus" has also been studied for its potential use in bioremediation and as a source of novel enzymes and bioactive compounds with potential applications in medicine and industry.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Disulfides are a type of organic compound that contains a sulfur-sulfur bond. In the context of biochemistry and medicine, disulfide bonds are often found in proteins, where they play a crucial role in maintaining their three-dimensional structure and function. These bonds form when two sulfhydryl groups (-SH) on cysteine residues within a protein molecule react with each other, releasing a molecule of water and creating a disulfide bond (-S-S-) between the two cysteines. Disulfide bonds can be reduced back to sulfhydryl groups by various reducing agents, which is an important process in many biological reactions. The formation and reduction of disulfide bonds are critical for the proper folding, stability, and activity of many proteins, including those involved in various physiological processes and diseases.

Pancreatic juice is an alkaline fluid secreted by the exocrine component of the pancreas, primarily containing digestive enzymes such as amylase, lipase, and trypsin. These enzymes aid in the breakdown of carbohydrates, fats, and proteins, respectively, in the small intestine during the digestion process. The bicarbonate ions present in pancreatic juice help neutralize the acidic chyme that enters the duodenum from the stomach, creating an optimal environment for enzymatic activity.

"Plant proteins" refer to the proteins that are derived from plant sources. These can include proteins from legumes such as beans, lentils, and peas, as well as proteins from grains like wheat, rice, and corn. Other sources of plant proteins include nuts, seeds, and vegetables.

Plant proteins are made up of individual amino acids, which are the building blocks of protein. While animal-based proteins typically contain all of the essential amino acids that the body needs to function properly, many plant-based proteins may be lacking in one or more of these essential amino acids. However, by consuming a variety of plant-based foods throughout the day, it is possible to get all of the essential amino acids that the body needs from plant sources alone.

Plant proteins are often lower in calories and saturated fat than animal proteins, making them a popular choice for those following a vegetarian or vegan diet, as well as those looking to maintain a healthy weight or reduce their risk of chronic diseases such as heart disease and cancer. Additionally, plant proteins have been shown to have a number of health benefits, including improving gut health, reducing inflammation, and supporting muscle growth and repair.

Amylases are enzymes that break down complex carbohydrates, such as starch and glycogen, into simpler sugars like maltose, glucose, and maltotriose. There are several types of amylases found in various organisms, including humans.

In humans, amylases are produced by the pancreas and salivary glands. Pancreatic amylase is released into the small intestine where it helps to digest dietary carbohydrates. Salivary amylase, also known as alpha-amylase, is secreted into the mouth and begins breaking down starches in food during chewing.

Deficiency or absence of amylases can lead to difficulties in digesting carbohydrates and may cause symptoms such as bloating, diarrhea, and abdominal pain. Elevated levels of amylase in the blood may indicate conditions such as pancreatitis, pancreatic cancer, or other disorders affecting the pancreas.

Tosylarginine Methyl Ester (TAME) is not a medication or a therapeutic agent, but it is a research compound used in scientific studies. It is a synthetic molecule that is often used as a control or a reference standard in enzyme inhibition assays. TAME is an esterified form of the amino acid arginine, with a tosyl group (p-toluenesulfonyl) attached to the nitrogen atom.

TAME is specifically used as a selective and reversible inhibitor of the enzyme called butyrylcholinesterase (BChE), which is involved in the breakdown of certain neurotransmitters in the body. By inhibiting BChE, TAME can help to increase the levels of these neurotransmitters in the brain, making it a useful tool for studying the mechanisms of this enzyme and its role in various physiological processes.

It's important to note that while TAME is used in research settings, it is not approved for use as a drug or therapeutic agent in humans or animals.

Alpha 1-antitrypsin (AAT, or α1-antiproteinase, A1AP) is a protein that is primarily produced by the liver and released into the bloodstream. It belongs to a group of proteins called serine protease inhibitors, which help regulate inflammation and protect tissues from damage caused by enzymes involved in the immune response.

Alpha 1-antitrypsin is particularly important for protecting the lungs from damage caused by neutrophil elastase, an enzyme released by white blood cells called neutrophils during inflammation. In the lungs, AAT binds to and inhibits neutrophil elastase, preventing it from degrading the extracellular matrix and damaging lung tissue.

Deficiency in alpha 1-antitrypsin can lead to chronic obstructive pulmonary disease (COPD) and liver disease. The most common cause of AAT deficiency is a genetic mutation that results in abnormal folding and accumulation of the protein within liver cells, leading to reduced levels of functional AAT in the bloodstream. This condition is called alpha 1-antitrypsin deficiency (AATD) and can be inherited in an autosomal codominant manner. Individuals with severe AATD may require augmentation therapy with intravenous infusions of purified human AAT to help prevent lung damage.

Kallikreins are a group of serine proteases, which are enzymes that help to break down other proteins. They are found in various tissues and body fluids, including the pancreas, kidneys, and saliva. In the body, kallikreins play important roles in several physiological processes, such as blood pressure regulation, inflammation, and fibrinolysis (the breakdown of blood clots).

There are two main types of kallikreins: tissue kallikreins and plasma kallikreins. Tissue kallikreins are primarily involved in the activation of kininogen, a protein that leads to the production of bradykinin, a potent vasodilator that helps regulate blood pressure. Plasma kallikreins, on the other hand, play a key role in the coagulation cascade by activating factors XI and XII, which ultimately lead to the formation of a blood clot.

Abnormal levels or activity of kallikreins have been implicated in various diseases, including cancer, cardiovascular disease, and inflammatory disorders. For example, some studies suggest that certain tissue kallikreins may promote tumor growth and metastasis, while others indicate that they may have protective effects against cancer. Plasma kallikreins have also been linked to the development of thrombosis (blood clots) and inflammation in cardiovascular disease.

Overall, kallikreins are important enzymes with diverse functions in the body, and their dysregulation has been associated with various pathological conditions.

Carboxypeptidases A are a group of enzymes that play a role in the digestion of proteins. They are found in various organisms, including humans, and function to cleave specific amino acids from the carboxyl-terminal end of protein substrates. In humans, Carboxypeptidase A is primarily produced in the pancreas and secreted into the small intestine as an inactive zymogen called procarboxypeptidase A.

Procarboxypeptidase A is activated by trypsin, another proteolytic enzyme, to form Carboxypeptidase A1 and Carboxypeptidase A2. These enzymes have different substrate specificities, with Carboxypeptidase A1 preferentially cleaving aromatic amino acids such as phenylalanine and tyrosine, while Carboxypeptidase A2 cleaves basic amino acids such as arginine and lysine.

Carboxypeptidases A play a crucial role in the final stages of protein digestion by breaking down large peptides into smaller di- and tripeptides, which can then be absorbed by the intestinal epithelium and transported to other parts of the body for use as building blocks or energy sources.

Peptides are short chains of amino acid residues linked by covalent bonds, known as peptide bonds. They are formed when two or more amino acids are joined together through a condensation reaction, which results in the elimination of a water molecule and the formation of an amide bond between the carboxyl group of one amino acid and the amino group of another.

Peptides can vary in length from two to about fifty amino acids, and they are often classified based on their size. For example, dipeptides contain two amino acids, tripeptides contain three, and so on. Oligopeptides typically contain up to ten amino acids, while polypeptides can contain dozens or even hundreds of amino acids.

Peptides play many important roles in the body, including serving as hormones, neurotransmitters, enzymes, and antibiotics. They are also used in medical research and therapeutic applications, such as drug delivery and tissue engineering.

Carboxypeptidases are a group of enzymes that catalyze the cleavage of peptide bonds at the carboxyl-terminal end of polypeptides or proteins. They specifically remove the last amino acid residue from the protein chain, provided that it has a free carboxyl group and is not blocked by another chemical group. Carboxypeptidases are classified into two main types based on their catalytic mechanism: serine carboxypeptidases and metallo-carboxypeptidases.

Serine carboxypeptidases, also known as chymotrypsin C or carboxypeptidase C, use a serine residue in their active site to catalyze the hydrolysis of peptide bonds. They are found in various organisms, including animals and bacteria.

Metallo-carboxypeptidases, on the other hand, require a metal ion (usually zinc) for their catalytic activity. They can be further divided into several subtypes based on their structure and substrate specificity. For example, carboxypeptidase A prefers to cleave hydrophobic amino acids from the carboxyl-terminal end of proteins, while carboxypeptidase B specifically removes basic residues (lysine or arginine).

Carboxypeptidases have important roles in various biological processes, such as protein maturation, digestion, and regulation of blood pressure. Dysregulation of these enzymes has been implicated in several diseases, including cancer, neurodegenerative disorders, and cardiovascular disease.

Enzyme precursors are typically referred to as zymogens or proenzymes. These are inactive forms of enzymes that can be activated under specific conditions. When the need for the enzyme's function arises, the proenzyme is converted into its active form through a process called proteolysis, where it is cleaved by another enzyme. This mechanism helps control and regulate the activation of certain enzymes in the body, preventing unwanted or premature reactions. A well-known example of an enzyme precursor is trypsinogen, which is converted into its active form, trypsin, in the digestive system.

Glycoproteins are complex proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. These glycans are linked to the protein through asparagine residues (N-linked) or serine/threonine residues (O-linked). Glycoproteins play crucial roles in various biological processes, including cell recognition, cell-cell interactions, cell adhesion, and signal transduction. They are widely distributed in nature and can be found on the outer surface of cell membranes, in extracellular fluids, and as components of the extracellular matrix. The structure and composition of glycoproteins can vary significantly depending on their function and location within an organism.

Fibrinolysin is defined as a proteolytic enzyme that dissolves or breaks down fibrin, a protein involved in the clotting of blood. This enzyme is produced by certain cells, such as endothelial cells that line the interior surface of blood vessels, and is an important component of the body's natural mechanism for preventing excessive blood clotting and maintaining blood flow.

Fibrinolysin works by cleaving specific bonds in the fibrin molecule, converting it into soluble degradation products that can be safely removed from the body. This process is known as fibrinolysis, and it helps to maintain the balance between clotting and bleeding in the body.

In medical contexts, fibrinolysin may be used as a therapeutic agent to dissolve blood clots that have formed in the blood vessels, such as those that can occur in deep vein thrombosis or pulmonary embolism. It is often administered in combination with other medications that help to enhance its activity and specificity for fibrin.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Macromolecular substances, also known as macromolecules, are large, complex molecules made up of repeating subunits called monomers. These substances are formed through polymerization, a process in which many small molecules combine to form a larger one. Macromolecular substances can be naturally occurring, such as proteins, DNA, and carbohydrates, or synthetic, such as plastics and synthetic fibers.

In the context of medicine, macromolecular substances are often used in the development of drugs and medical devices. For example, some drugs are designed to bind to specific macromolecules in the body, such as proteins or DNA, in order to alter their function and produce a therapeutic effect. Additionally, macromolecular substances may be used in the creation of medical implants, such as artificial joints and heart valves, due to their strength and durability.

It is important for healthcare professionals to have an understanding of macromolecular substances and how they function in the body, as this knowledge can inform the development and use of medical treatments.

In the context of medicine, "chemistry" often refers to the field of study concerned with the properties, composition, and structure of elements and compounds, as well as their reactions with one another. It is a fundamental science that underlies much of modern medicine, including pharmacology (the study of drugs), toxicology (the study of poisons), and biochemistry (the study of the chemical processes that occur within living organisms).

In addition to its role as a basic science, chemistry is also used in medical testing and diagnosis. For example, clinical chemistry involves the analysis of bodily fluids such as blood and urine to detect and measure various substances, such as glucose, cholesterol, and electrolytes, that can provide important information about a person's health status.

Overall, chemistry plays a critical role in understanding the mechanisms of diseases, developing new treatments, and improving diagnostic tests and techniques.

"Swine" is a common term used to refer to even-toed ungulates of the family Suidae, including domestic pigs and wild boars. However, in a medical context, "swine" often appears in the phrase "swine flu," which is a strain of influenza virus that typically infects pigs but can also cause illness in humans. The 2009 H1N1 pandemic was caused by a new strain of swine-origin influenza A virus, which was commonly referred to as "swine flu." It's important to note that this virus is not transmitted through eating cooked pork products; it spreads from person to person, mainly through respiratory droplets produced when an infected person coughs or sneezes.

Chemical phenomena refer to the changes and interactions that occur at the molecular or atomic level when chemicals are involved. These phenomena can include chemical reactions, in which one or more substances (reactants) are converted into different substances (products), as well as physical properties that change as a result of chemical interactions, such as color, state of matter, and solubility. Chemical phenomena can be studied through various scientific disciplines, including chemistry, biochemistry, and physics.

In a medical context, "hot temperature" is not a standard medical term with a specific definition. However, it is often used in relation to fever, which is a common symptom of illness. A fever is typically defined as a body temperature that is higher than normal, usually above 38°C (100.4°F) for adults and above 37.5-38°C (99.5-101.3°F) for children, depending on the source.

Therefore, when a medical professional talks about "hot temperature," they may be referring to a body temperature that is higher than normal due to fever or other causes. It's important to note that a high environmental temperature can also contribute to an elevated body temperature, so it's essential to consider both the body temperature and the environmental temperature when assessing a patient's condition.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Immobilized enzymes refer to enzymes that have been restricted or fixed in a specific location and are unable to move freely. This is typically achieved through physical or chemical methods that attach the enzyme to a solid support or matrix. The immobilization of enzymes can provide several advantages, including increased stability, reusability, and ease of separation from the reaction mixture.

Immobilized enzymes are widely used in various industrial applications, such as biotransformations, biosensors, and diagnostic kits. They can also be used for the production of pharmaceuticals, food additives, and other fine chemicals. The immobilization techniques include adsorption, covalent binding, entrapment, and cross-linking.

Adsorption involves physically attaching the enzyme to a solid support through weak forces such as van der Waals interactions or hydrogen bonding. Covalent binding involves forming chemical bonds between the enzyme and the support matrix. Entrapment involves encapsulating the enzyme within a porous matrix, while cross-linking involves chemically linking multiple enzyme molecules together to form a stable structure.

Overall, immobilized enzymes offer several advantages over free enzymes, including improved stability, reusability, and ease of separation from the reaction mixture, making them valuable tools in various industrial applications.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

Chymotrypsinogen is the inactive precursor form of the enzyme chymotrypsin, which is produced in the pancreas and plays a crucial role in digesting proteins in the small intestine. This zymogen is activated when it is cleaved by another protease called trypsin, resulting in the formation of the active enzyme chymotrypsin. Chymotrypsinogen is synthesized and stored in the pancreas as a proenzyme to prevent premature activation and potential damage to the pancreatic tissue. Once released into the small intestine, trypsin-mediated cleavage of chymotrypsinogen leads to the formation of chymotrypsin, which then contributes to protein breakdown and absorption in the gut.

Intestinal secretions refer to the fluids and electrolytes that are released by the cells lining the small intestine in response to various stimuli. These secretions play a crucial role in the digestion and absorption of nutrients from food. The major components of intestinal secretions include water, electrolytes (such as sodium, chloride, bicarbonate, and potassium), and enzymes that help break down carbohydrates, proteins, and fats.

The small intestine secretes these substances in response to hormonal signals, neural stimulation, and the presence of food in the lumen of the intestine. The secretion of water and electrolytes helps maintain the proper hydration and pH of the intestinal contents, while the enzymes facilitate the breakdown of nutrients into smaller molecules that can be absorbed across the intestinal wall.

Abnormalities in intestinal secretions can lead to various gastrointestinal disorders, such as diarrhea, malabsorption, and inflammatory bowel disease.

Affinity chromatography is a type of chromatography technique used in biochemistry and molecular biology to separate and purify proteins based on their biological characteristics, such as their ability to bind specifically to certain ligands or molecules. This method utilizes a stationary phase that is coated with a specific ligand (e.g., an antibody, antigen, receptor, or enzyme) that selectively interacts with the target protein in a sample.

The process typically involves the following steps:

1. Preparation of the affinity chromatography column: The stationary phase, usually a solid matrix such as agarose beads or magnetic beads, is modified by covalently attaching the ligand to its surface.
2. Application of the sample: The protein mixture is applied to the top of the affinity chromatography column, allowing it to flow through the stationary phase under gravity or pressure.
3. Binding and washing: As the sample flows through the column, the target protein selectively binds to the ligand on the stationary phase, while other proteins and impurities pass through. The column is then washed with a suitable buffer to remove any unbound proteins and contaminants.
4. Elution of the bound protein: The target protein can be eluted from the column using various methods, such as changing the pH, ionic strength, or polarity of the buffer, or by introducing a competitive ligand that displaces the bound protein.
5. Collection and analysis: The eluted protein fraction is collected and analyzed for purity and identity, often through techniques like SDS-PAGE or mass spectrometry.

Affinity chromatography is a powerful tool in biochemistry and molecular biology due to its high selectivity and specificity, enabling the efficient isolation of target proteins from complex mixtures. However, it requires careful consideration of the binding affinity between the ligand and the protein, as well as optimization of the elution conditions to minimize potential damage or denaturation of the purified protein.

I believe there may be some confusion in your question. "Rabbits" is a common name used to refer to the Lagomorpha species, particularly members of the family Leporidae. They are small mammals known for their long ears, strong legs, and quick reproduction.

However, if you're referring to "rabbits" in a medical context, there is a term called "rabbit syndrome," which is a rare movement disorder characterized by repetitive, involuntary movements of the fingers, resembling those of a rabbit chewing. It is also known as "finger-chewing chorea." This condition is usually associated with certain medications, particularly antipsychotics, and typically resolves when the medication is stopped or adjusted.

Gabexate is a medicinal drug that belongs to the class of agents known as serine protease inhibitors. It is used in the treatment and prevention of inflammation and damage to tissues caused by various surgical procedures, pancreatitis, and other conditions associated with the activation of proteolytic enzymes.

Gabexate works by inhibiting the activity of certain enzymes such as trypsin, chymotrypsin, and thrombin, which play a key role in the inflammatory response and blood clotting cascade. By doing so, it helps to reduce the release of inflammatory mediators, prevent further tissue damage, and promote healing.

Gabexate is available in various forms, including injectable solutions and enteric-coated tablets, and its use is typically reserved for clinical settings under the supervision of a healthcare professional. As with any medication, it should be used only under the direction of a qualified medical practitioner, and its potential benefits and risks should be carefully weighed against those of other available treatment options.

Thrombin is a serine protease enzyme that plays a crucial role in the coagulation cascade, which is a complex series of biochemical reactions that leads to the formation of a blood clot (thrombus) to prevent excessive bleeding during an injury. Thrombin is formed from its precursor protein, prothrombin, through a process called activation, which involves cleavage by another enzyme called factor Xa.

Once activated, thrombin converts fibrinogen, a soluble plasma protein, into fibrin, an insoluble protein that forms the structural framework of a blood clot. Thrombin also activates other components of the coagulation cascade, such as factor XIII, which crosslinks and stabilizes the fibrin network, and platelets, which contribute to the formation and growth of the clot.

Thrombin has several regulatory mechanisms that control its activity, including feedback inhibition by antithrombin III, a plasma protein that inactivates thrombin and other serine proteases, and tissue factor pathway inhibitor (TFPI), which inhibits the activation of factor Xa, thereby preventing further thrombin formation.

Overall, thrombin is an essential enzyme in hemostasis, the process that maintains the balance between bleeding and clotting in the body. However, excessive or uncontrolled thrombin activity can lead to pathological conditions such as thrombosis, atherosclerosis, and disseminated intravascular coagulation (DIC).

Pancreatitis is a medical condition characterized by inflammation of the pancreas, a gland located in the abdomen that plays a crucial role in digestion and regulating blood sugar levels. The inflammation can be acute (sudden and severe) or chronic (persistent and recurring), and it can lead to various complications if left untreated.

Acute pancreatitis often results from gallstones or excessive alcohol consumption, while chronic pancreatitis may be caused by long-term alcohol abuse, genetic factors, autoimmune conditions, or metabolic disorders like high triglyceride levels. Symptoms of acute pancreatitis include severe abdominal pain, nausea, vomiting, fever, and increased heart rate, while chronic pancreatitis may present with ongoing abdominal pain, weight loss, diarrhea, and malabsorption issues due to impaired digestive enzyme production. Treatment typically involves supportive care, such as intravenous fluids, pain management, and addressing the underlying cause. In severe cases, hospitalization and surgery may be necessary.

I'm sorry for any confusion, but "soybeans" are not a medical term. They are a type of legume that is commonly used in agriculture and food production. The medical community might discuss soybeans in the context of nutrition or allergies, but there isn't a formal medical definition for this term.

Here's some general information: Soybeans, scientifically known as Glycine max, are native to East Asia and are now grown worldwide. They are a significant source of plant-based protein and oil. Soybeans contain various nutrients, including essential amino acids, fiber, B vitamins, and minerals like calcium, iron, magnesium, and zinc. They are used in various food products such as tofu, soy milk, tempeh, and miso. Additionally, soybeans are also used in the production of industrial products, including biodiesel, plastics, and inks. Some people may have allergic reactions to soybeans or soy products.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

In medical terms, "seeds" are often referred to as a small amount of a substance, such as a radioactive material or drug, that is inserted into a tissue or placed inside a capsule for the purpose of treating a medical condition. This can include procedures like brachytherapy, where seeds containing radioactive materials are used in the treatment of cancer to kill cancer cells and shrink tumors. Similarly, in some forms of drug delivery, seeds containing medication can be used to gradually release the drug into the body over an extended period of time.

It's important to note that "seeds" have different meanings and applications depending on the medical context. In other cases, "seeds" may simply refer to small particles or structures found in the body, such as those present in the eye's retina.

Microbial collagenase is not a medical term per se, but it does refer to an enzyme that is used in various medical and research contexts. Collagenases are a group of enzymes that break down collagen, a structural protein found in connective tissues such as skin, tendons, and ligaments. Microbial collagenase is a type of collagenase that is produced by certain bacteria, such as Clostridium histolyticum.

In medical terms, microbial collagenase is used in various therapeutic and research applications, including:

1. Wound healing: Microbial collagenase can be used to break down and remove necrotic tissue from wounds, which can help promote healing and prevent infection.
2. Dental applications: Collagenases have been used in periodontal therapy to remove calculus and improve the effectiveness of root planing and scaling procedures.
3. Research: Microbial collagenase is a valuable tool for researchers studying the structure and function of collagen and other extracellular matrix proteins. It can be used to digest tissue samples, allowing scientists to study the individual components of the extracellular matrix.

It's important to note that while microbial collagenase has many useful applications, it must be used with care, as excessive or improper use can damage healthy tissues and cause adverse effects.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Oligopeptides are defined in medicine and biochemistry as short chains of amino acids, typically containing fewer than 20 amino acid residues. These small peptides are important components in various biological processes, such as serving as signaling molecules, enzyme inhibitors, or structural elements in some proteins. They can be found naturally in foods and may also be synthesized for use in medical research and therapeutic applications.

Ion exchange chromatography is a type of chromatography technique used to separate and analyze charged molecules (ions) based on their ability to exchange bound ions in a solid resin or gel with ions of similar charge in the mobile phase. The stationary phase, often called an ion exchanger, contains fixed ated functional groups that can attract counter-ions of opposite charge from the sample mixture.

In this technique, the sample is loaded onto an ion exchange column containing the charged resin or gel. As the sample moves through the column, ions in the sample compete for binding sites on the stationary phase with ions already present in the column. The ions that bind most strongly to the stationary phase will elute (come off) slower than those that bind more weakly.

Ion exchange chromatography can be performed using either cation exchangers, which exchange positive ions (cations), or anion exchangers, which exchange negative ions (anions). The pH and ionic strength of the mobile phase can be adjusted to control the binding and elution of specific ions.

Ion exchange chromatography is widely used in various applications such as water treatment, protein purification, and chemical analysis.

Acrosin is a proteolytic enzyme that is found in the acrosome, which is a cap-like structure located on the anterior part of the sperm head. This enzyme plays an essential role in the fertilization process by helping the sperm to penetrate the zona pellucida, which is the glycoprotein coat surrounding the egg.

Acrosin is released from the acrosome when the sperm encounters the zona pellucida, and it begins to digest the glycoproteins in the zona pellucida, creating a path for the sperm to reach and fuse with the egg's plasma membrane. This enzyme is synthesized and stored in the acrosome during spermatogenesis and is activated during the acrosome reaction, which is a critical event in fertilization.

Defects in acrosin function or regulation have been implicated in male infertility, making it an important area of research in reproductive biology.

Protease-activated receptor 1 (PAR-1) is a type of G protein-coupled receptor that is activated by proteolytic cleavage rather than by binding to a ligand in the traditional sense. PAR-1 is expressed on the surface of various cell types, including endothelial cells, smooth muscle cells, and platelets.

When activated by proteases such as thrombin or trypsin, PAR-1 undergoes a conformational change that allows it to interact with G proteins and initiate intracellular signaling pathways. These pathways can lead to a variety of cellular responses, including platelet activation, smooth muscle contraction, and inflammation.

PAR-1 has been implicated in several physiological processes, including hemostasis, thrombosis, and vascular remodeling, as well as in the pathophysiology of various diseases, such as atherosclerosis, cancer, and Alzheimer's disease. Therefore, PAR-1 is an important target for the development of therapeutic agents for these conditions.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

A Structure-Activity Relationship (SAR) in the context of medicinal chemistry and pharmacology refers to the relationship between the chemical structure of a drug or molecule and its biological activity or effect on a target protein, cell, or organism. SAR studies aim to identify patterns and correlations between structural features of a compound and its ability to interact with a specific biological target, leading to a desired therapeutic response or undesired side effects.

By analyzing the SAR, researchers can optimize the chemical structure of lead compounds to enhance their potency, selectivity, safety, and pharmacokinetic properties, ultimately guiding the design and development of novel drugs with improved efficacy and reduced toxicity.

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

Temperature, in a medical context, is a measure of the degree of hotness or coldness of a body or environment. It is usually measured using a thermometer and reported in degrees Celsius (°C), degrees Fahrenheit (°F), or kelvin (K). In the human body, normal core temperature ranges from about 36.5-37.5°C (97.7-99.5°F) when measured rectally, and can vary slightly depending on factors such as time of day, physical activity, and menstrual cycle. Elevated body temperature is a common sign of infection or inflammation, while abnormally low body temperature can indicate hypothermia or other medical conditions.

Mass spectrometry (MS) is an analytical technique used to identify and quantify the chemical components of a mixture or compound. It works by ionizing the sample, generating charged molecules or fragments, and then measuring their mass-to-charge ratio in a vacuum. The resulting mass spectrum provides information about the molecular weight and structure of the analytes, allowing for identification and characterization.

In simpler terms, mass spectrometry is a method used to determine what chemicals are present in a sample and in what quantities, by converting the chemicals into ions, measuring their masses, and generating a spectrum that shows the relative abundances of each ion type.

Cucurbitaceae is the scientific name for the gourd family of plants, which includes a variety of vegetables and fruits such as cucumbers, melons, squashes, and pumpkins. These plants are characterized by their trailing or climbing growth habits and their large, fleshy fruits that have hard seeds enclosed in a protective coat. The fruits of these plants are often used as food sources, while other parts of the plant may also have various uses such as medicinal or ornamental purposes.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

... 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 ...
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. ...
"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 ...
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 ...
... 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 ...
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 ...
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 ...
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: ...
... trypsin, and lipase. These are measured by a catheter placed in the duodenum. Cholecystokinin also stimulates the flow of bile ...
... 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. ( ...
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 ...
A study with immobilized trypsin". FEBS Lett. 232 (2): 281-5. doi:10.1016/0014-5793(88)80753-1. PMID 3378620. S2CID 44333810. ...
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 ( ...
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 ...
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 ...
A study with immobilized trypsin". FEBS Letters. 232 (2): 281-5. doi:10.1016/0014-5793(88)80753-1. PMID 3378620. S2CID 44333810 ...
"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 ...
Trypsin Lys-N Jekel, PA; Weijer, WJ; Beintema, JJ (15 October 1983). "Use of endoproteinase Lys-C from Lysobacter enzymogenes ...
... 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 ...
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, ...
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 ...
"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): ...
This gene encodes a trypsin inhibitor. The protein shares similarity to insect venom allergens, mammalian testis-specific ...
Neurath's work on proteolytic enzymes included studies of trypsin, carboxypeptidase and thermolysin. Neurath also studied other ... "The specific esterase activity of trypsin". J. Biol. Chem. 172 (1): 221-239. Bradshaw, R. A.; Ericsson, L. H.; Walsh, K. A.; ...
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, ...
... is the assortment of peptides formed by the digestion of casein by the protease trypsin. Tryptone is commonly used in ... Biology portal Albumose Trypticase soy agar Fraser, Dean; Powell, Richard (1950). "The Kinetics of Trypsin Digestion" (PDF). ...
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, ...
Homology with the trypsin/kallikrein gene family". The Journal of Biological Chemistry. 263 (16): 7628-31. doi:10.1016/S0021- ...
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 ...
The Chemistry of Pepsin, Trypsin, and Bacteriophage. Columbia University Press, New York. OCLC 2387455 d'Hérelle, F. 1938. Le ...
Trypsin 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 ...
Cationic trypsinCALCIUM IONGLYCEROLN-cyclooctylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
The binding of a series of low molecular weight ligands towards trypsin and thrombin has been studied by isothermal titration ... The binding of a series of low molecular weight ligands towards trypsin and thrombin has been studied by isothermal titration ... Crystal Structures of Factor Xa Specific Inhibitors in Complex with Trypsin: Structural Grounds for Inhibition of Factor Xa and ... Structural and Functional Analyses of Benzamidine-Based Inhibitors in Complex with Trypsin: Implications for the Inhibition of ...
Pancreatic trypsin and trypsin-2 were almost equally effective at cleaving PAR-2 suggesting that extrapancreatic trypsins are ... Extrapancreatic trypsin-2 cleaves proteinase-activated receptor-2 Biochem Biophys Res Commun. 2000 Aug 18;275(1):77-83. doi: ... but were much less potent than pancreatic trypsin and trypsin-2 isolated from a carcinoma cell line. ...
English Translation for trypsin inhibitor - dict.cc German-English Dictionary ... trypsin. Trypsin {n}. pharm.. cyclooxygenase-2 inhibitor ,COX-2 inhibitor, [coxibe]. Cyclooxygenase-2-Inhibitor {m}. ,COX-2- ... trypsin. • trypsin inhibitor. trypsinogen. tryptamine. tryptaminergic. tryptase. tryptathionine. tryptic. tryptophan. ... Search forum for trypsin inhibitor. » Ask forum members for trypsin inhibitor. Recent Searches ...
Continuously check the level of the trypsin solution and add additional trypsin solution or buffer as needed. ... The trypsin solution will be pulled into the gel as it swells. If the gel was Coomassie-stained, add more trypsin in order to ... Mix the solution thoroughly to ensure complete dissolution of the trypsin.. *Add the trypsin solution to each sample tube in an ... Continuously check the level of the trypsin solution and add additional trypsin solution or buffer as needed. ...
Trypsin and chymotrypsin in stool Trypsin and chymotrypsin are substances released from the pancreas during normal digestion. ... Trypsin aids in digestion by cutting protein chains at ... arginine or lysine, which breaks down the protein. Trypsin also ... cleaved) into its working or active form called trypsin. When digestion is complete and trypsin is no longer needed, the enzyme ... Trypsinogen is converted to trypsin. Then it starts the process needed to break ... Chernecky CC, Berger BJ. Trypsin- plasma or ...
A mixture of Trypsin and rLys-C designed to improve digestion of proteins or protein mixtures in solution. ... Incomplete digestion with trypsin was evident after comparing peptide peak intensities in trypsin and Trypsin/Lys-C Mix digests ... Improved Reproducibility using Trypsin/Lys-C. Improved reproducibility of IgG (Rituximab) digestion when using the Trypsin/Lys- ... Efficient digestion with Trypsin/Lys-C Mix in the presence of trypsin-inhibiting agents. Yeast protein extract was used as a ...
... and highly reproducible trypsin protein digestion for peptide characterization and quantitation in biopharmaceutical protein ... SMART Digest Trypsin Kit, Soluble. SMART Digest Soluble Trypsin. SMART Digest Soluble Trypsin, SMART Digest Buffer, Collection ... SMART Digest Trypsin Kit, with Filter/Collection plate. SMART Digest Resin Pre-filled into PCR Tubes. SMART Digest Resin Pre- ... SMART Digest Trypsin Kit, with Collection plate. SMART Digest Resin Pre-filled into PCR Tubes. SMART Digest Resin Pre-filled ...
Trypsin Digestion Protocol using NEB Trypsin-ultra™ and the FASP Kit. *The starting material can be cells, proteome extracts, ... Trypsin-ultra has been found to have very low levels of autocleavage as compared to other MS grade trypsin. Therefore, using ... Typical solution based digests normally recommend a 1:50-1:100 trypsin to protein ratio; however, when using Trypsin-ultra and ... Home Protocols Trypsin Digestion Protocol using NEB Trypsin-ultra™ and the FASP Kit ...
Trypsin. PFAM accession number:. PF00089. Interpro abstract (IPR001254):. This entry represents the active-site-containing ... The domain within your query sequence starts at position 1 and ends at position 75; the E-value for the Trypsin domain shown ... The catalytic activity of the serine proteases from the trypsin family is provided by a charge relay system involving an ... For full annotation and more information, please see the PFAM entry Trypsin ...
Anionic trypsin variant S195A in complex with bovine pancreatic trypsin inhibitor (BPTI) cleaved at the scissile bond (LYS15- ... Anionic trypsin variant S195A in complex with bovine pancreatic trypsin inhibitor (BPTI) cleaved at the scissile bond (LYS15- ... Anionic trypsin-2. A [auth E]. 223. Rattus norvegicus. Mutation(s): 1 Gene Names: Prss2, Try2. EC: 3.4.21.4. ... Pancreatic trypsin inhibitor. B [auth I]. 15. N/A. Mutation(s): 0 ...
If you wish to reuse any or all of this article please use the link below which will take you to the Copyright Clearance Centers RightsLink service. You will be able to get a quick price and instant permission to reuse the content in many different ways.. ...
Trypsin. Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine ... Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, ... For mass spectrometry sequence analysis, we recommend our ultra-pure MSG-Trypsin™ that is specifically designed for mass ... This trypsin is purified from bovine pancreas, 1X crystallized, dialyzed against 1mM HCl and lyophilized. ...
Impact of UV-C pretreatment on β-lactoglobulin hydrolysis by trypsin: Production and bioavailability of bioactive peptides. ... by trypsin, peptide profile of tryptic hydrolysates by MALDI-TOF/TOF-MS, and bioavailability of β-lactoglobulin were compared. ... whereas thermal treatment produced aggregates that impede trypsin activity. Tryptic hydrolyses of UV-C light treated β- ...
Get up-to-date information on Trypsin side effects, uses, dosage, overdose, pregnancy, alcohol and more. Learn more about ... Trypsin is available in the following doses: *Balsam Peru/castor Oil/trypsin Topical 72.5 Mg-650 Mg-0.1 Mg/0.82 Ml Topical ... Balsam Peru/castor Oil/trypsin Topical 87 Mg-788 Mg-0.12 Mg/g Topical Gel*Balsam Peru/castor Oil/trypsin Topical 87 Mg-788 Mg- ... How was your experience with Trypsin?. First, a little about yourself. Male Female ...
... with BIs Trypsin EDTA Solution A (0.25%), EDTA (0.02%) ... Trypsin and Cell Dissociation > * Trypsin EDTA Solution A (0.25 ... Trypsin proteolysis or trypsinization is a process in which proteins have been digested or treated with trypsin and are thus ... Youre reviewing: Trypsin EDTA Solution A (0.25%), EDTA (0.02%) How do you rate this product? *. 1 star. 2 stars. 3 stars. 4 ... Trypsin is available in a varied array of formulations with or without EDTA. EDTA is a chelator that binds calcium and ...
... of the basic pancreatic trypsin inhibitor. Well-tempered metadynamics simulations were performed to estimate the ring-flipping ... of the basic pancreatic trypsin inhibitor. Well-tempered metadynamics simulations were performed to estimate the ring-flipping ...
Effects of soybean trypsin inhibitor on hypopharyngeal gland protein content, total midgut protease activity and survival of ... Effects of soybean trypsin inhibitor on hypopharyngeal gland protein content, total midgut protease activity and survival of ... Effects of soybean trypsin inhibitor on hypopharyngeal gland protein content, total midgut protease activity and survival of ...
Trypsin-Like Immunoreactivity Protein, Cobalamin & Folate Panel - Canine (ChL). Measurement of trypsin-like immunoreactivity ( ...
During the separation of trypsin inhibitors by size exclusion chromatography, trypsin-like activity was also observed, ... indicating the possible presence of an endogenous trypsin or similar protease in the pea seed. Between 6 and 10 trypsin ... Trypsin inhibitor activity (TIA) in New Zealand grown pea cultivars ranged from 0.33 to 0.75 TIU/mg DM; much lower than ... Total trypsin inhibition in New Zealand pea cultivars was found to be negatively correlated to tannin content. Thus it appears ...
Optimum Ph Of Trypsin Essay. It is hypothesized that the optimum pH of trypsin is 8. Three different pH levels were tested, and ... According to Lee et al the optimum TPCK-trypsin concentration that can be used to infect DF-1 cells with IAV is 0.1 mg/ml (Lee ... I am planning to try different concentrations of TPCK-trypsin to see which concentration will work better in order not to lose ... TPCK-trypsin helps the virus to infect the cell through cleaving the HA protein into HA1 and HA2. ...
Trypsin (serine protease) inhibitors in peanut genotypes aiming for control of stored grain pests.. pt_BR. ...
Gelatinolytic and anti-trypsin activities in seminal plasma of common carp: relationship to blood, skin mucus and spermatozoa. ...
Trypsin digestion. Recombinant purified proteins (0.5 mg/ml) were treated with 25 μg/ml of trypsin (SRL) for 1 h at 37 °C after ... B) trypsin digested proteins run onto denaturing SDS-PAGE. (C) same protein sample run onto the semi-native gel with and ... Trypsin digestion was carried out for one hour at 37 °C followed by further analysis via either SDS reducing PAGE or semi- ... Trypsin digestion analysis and ATR-FTIR spectroscopy of HomA and HomB. (A) pictorial representation of HomA and HomB protease ...
THE ESTIMATION OF PEPSIN, TRYPSIN, PAPAIN, AND CATHEPSIN WITH HEMOGLOBIN.. scientific article published on September 1938 ...
Trypsin Enzyme from Trypsin-Chymotrypsin - Shanghai Sunwise Chemical Co., Ltd. ... China Trypsin-Chymotrypsin, Find details about China DMF, ... Characters:Trypsin-Chymotrypsin is a white or yellowish powder ... Product Name: Trypsin-Chymotrypsin. Identification. Molecular Formula NA. Molecular Weight NA. CAS Number NA. EINECS/ELINCS NA ... Product Name: Trypsin-Chymotrypsin. Identification. Molecular Formula NA. Molecular Weight NA. CAS Number NA. EINECS/ELINCS NA ...
  • The trypsin then activates additional trypsin, chymotrypsin and carboxypeptidase. (wikipedia.org)
  • The activity of trypsin is not affected by the enzyme inhibitor tosyl phenylalanyl chloromethyl ketone, TPCK, which deactivates chymotrypsin. (wikipedia.org)
  • Trypsin and chymotrypsin are substances released from the pancreas during normal digestion. (nih.gov)
  • Your sample may also be tested for trypsin , an enzyme released by the pancreas along with chymotrypsin. (nih.gov)
  • Trypsin-Chymotrypsin is a white or yellowish powder having proteolytic activity. (sunwisechem.com)
  • TRYPSIN II is our low-endotoxin preparation with reduced chymotrypsin activity. (bioseutica.com)
  • TRYPSIN II is ideally suited to the food industry, as high chymotrypsin activity can hydrolyse aromatic amino acids which contribute to food flavour profiles. (bioseutica.com)
  • Recombinant Porcine Trypsin is free from foreign enzymes such as carboxypeptidase A & chymotrypsin. (angioproteomie.com)
  • We describe here a high-resolution (1.46 A) crystal structure of a complex formed between a cleaved form of bovine pancreatic trypsin inhibitor (BPTI) and a catalytically inactive trypsin variant with the BPTI cleavage site ideally positioned in the active site for resynthesis of the peptide bond. (rcsb.org)
  • In this study, we investigated the ability of the infrequent metadynamics approach to estimate the flip rate and discriminate between slow and fast ring flips for eight individual aromatic side chains (F4, Y10, Y21, F22, Y23, F33, Y35, and F45) of the basic pancreatic trypsin inhibitor. (lu.se)
  • Effects of soybean trypsin inhibitor on hypopharyngeal gland protein content, total midgut protease activity and survival of the honey bee (Apis mellifera L. (oregonstate.edu)
  • Seventeen New Zealand grown, spring and winter pea cultivars were assayed for trypsin inhibitor activity, tannin and protein content. (lincoln.ac.nz)
  • Phenotypic characteristics in relation to trypsin inhibitor activity and condensed tannin content were observed. (lincoln.ac.nz)
  • In general, marrowfat peas contained the highest levels of trypsin inhibitor activity and soluble protein whereas maple peas had low levels of soluble protein and trypsin inhibitor activity. (lincoln.ac.nz)
  • Center, Lund University, P.O. proteins bovine pancreatic trypsin inhibitor (BPTI) and ubiquitin. (lu.se)
  • For example, a molecular weight of 23.3 kDa is reported for trypsin from bovine and porcine sources. (wikipedia.org)
  • Recombinant Porcine Trypsin is free from any animal and human sources. (angioproteomie.com)
  • Recombinant Porcine Trypsin expressed in Yeast and purified by standard chromatography techniques. (angioproteomie.com)
  • Recombinant Porcine Trypsin should be stored at 2-8°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). (angioproteomie.com)
  • The Porcine Trypsin (2.98mg/ml) is formulated with 1mM HCl and 20mM CaCl2, pH-3. (angioproteomie.com)
  • Contains 0.5 g/L trypsin (from Porcine pancreas), 0.2 g/L EDTA·4Na and phenol red in HBSS without calcium and magnesium. (genedirex.com)
  • The trypsin is an enzyme of porcine origin. (who.int)
  • At no time the final polio vaccine virus which is in the vaccine vial comes in contact with Trypsin nor any other porcine product. (who.int)
  • During the separation of trypsin inhibitors by size exclusion chromatography, trypsin-like activity was also observed, indicating the possible presence of an endogenous trypsin or similar protease in the pea seed. (lincoln.ac.nz)
  • Alice: Trypsin (serine protease) inhibitors in peanut genotypes aiming for control of stored grain pests. (embrapa.br)
  • Recombinant Human Trypsin is free from protease inhibitors such as PMSF and EDTA. (angioproteomie.com)
  • Trypsin TPCK-Treated is a high quality TPCK-Treated Trypsin, a serine protease that specifically hydrolyzes peptide bonds at the carboxyl side of Lysine and Arginine residues. (moleculardepot.com)
  • Human Trypsin, Recombinant Enzyme, For Sale, For Cell Culture Cell culture - Human Trypsin Description Trypsin is a member of the serine protease family. (recombinanttrypsin.com)
  • Cell Dissociation Solution, Expressed in E.coli, Dissociate Cells Recombinant Trypsin Solution Description Trypsin is a member of the serine protease family. (recombinanttrypsin.com)
  • Trypsin, Stem Cell Culture, Clinic Cell Therapy, Animal Origin Free, Human Trypsin Human Tryspsin Description Trypsin is a member of the serine protease family. (recombinanttrypsin.com)
  • In cell culture , RVAs are propagated in culture medium supplemented with the exogenous protease trypsin , which cleaves VP4 and induces the maturation of progeny RVA virions . (bvsalud.org)
  • Mass spectrometry and amino-terminal sequence analysis identified the purified protease as chicken trypsin II P29. (cdc.gov)
  • This means that trypsin predominantly cleaves proteins at the carboxyl side (or "C-terminal side") of the amino acids lysine and arginine except when either is bound to a C-terminal proline, although large-scale mass spectrometry data suggest cleavage occurs even with proline. (wikipedia.org)
  • Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues. (gbiosciences.com)
  • Two different mast cell tryptases cleaved PAR-2 in a concentration dependent manner, but were much less potent than pancreatic trypsin and trypsin-2 isolated from a carcinoma cell line. (nih.gov)
  • Pancreatic trypsin and trypsin-2 were almost equally effective at cleaving PAR-2 suggesting that extrapancreatic trypsins are potential in vivo activators of PAR-2. (nih.gov)
  • Abbreviations used: BPTI, bovine pancreatic trypsin atoms in carboxyl (Lankhorst et al . (lu.se)
  • The process is commonly referred to as trypsin proteolysis or trypsinization, and proteins that have been digested/treated with trypsin are said to have been trypsinized. (wikipedia.org)
  • Trypsin proteolysis or trypsinization is a process in which proteins have been digested or treated with trypsin and are thus said to be trypsinized. (bioind.com)
  • Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces. (wikipedia.org)
  • Once in the small intestine, the enzyme enterokinase (also called enteropeptidase) activates trypsinogen into trypsin by proteolytic cleavage. (wikipedia.org)
  • The negative aspartate residue (Asp 189) located in the catalytic pocket (S1) of trypsin is responsible for attracting and stabilizing positively charged lysine and/or arginine, and is, thus, responsible for the specificity of the enzyme. (wikipedia.org)
  • cationic trypsinogen enzyme that is prematurely converted to trypsin while it is still in the pancreas. (nih.gov)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Pig Trypsin (TRY) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids with no significant corss-reactivity with analogues from other species. (orbitalbiosciences.com)
  • The binding of a series of low molecular weight ligands towards trypsin and thrombin has been studied by isothermal titration calorimetry and protein crystallography. (rcsb.org)
  • Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. (wikipedia.org)
  • Trypsin was discovered in 1876 by Wilhelm Kühne and was named from the Ancient Greek word for rubbing since it was first isolated by rubbing the pancreas with glycerin. (wikipedia.org)
  • Trypsin is produced as the inactive zymogen trypsinogen in the pancreas. (wikipedia.org)
  • This trypsin is purified from bovine pancreas, 1X crystallized, dialyzed against 1mM HCl and lyophilized. (gbiosciences.com)
  • Host serine proteases TMPRSS2 and TMPRSS11D mediate proteolytic activation and trypsin-independent infection in group A rotaviruses. (bvsalud.org)
  • This experiment is still under optimization, I keep losing cells after infection and this might be due to the addition of TPCK-trypsin (L-(tosylamido-2-phenyl) ethyl chloromethyl ketone). (cram.com)
  • EDTA is a chelator that binds calcium and magnesium ions that may otherwise inhibit the trypsin activity, which then hydrolyzes and gains access to the intercellular bonds (cell-cell and/or cell-substrate bonds). (bioind.com)
  • Trypsin specifically hydrolyzes amides, peptides and proteins at the C-terminus side of arginine and lysine residues. (emdmillipore.com)
  • Human trypsin has an optimal operating temperature of about 37 °C. In contrast, the Atlantic cod has several types of trypsins for the poikilotherm fish to survive at different body temperatures. (wikipedia.org)
  • Continuously check the level of the trypsin solution and add additional trypsin solution or buffer as needed. (biosyn.com)
  • In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into smaller peptides. (wikipedia.org)
  • Biological Industries' Trypsin is designed to gently dissociate cells from almost any support substrates, as well as from each other, in order to actualize cell manipulation techniques, and for other studies that require intact cell-surface proteins. (bioind.com)
  • CHYMOTEX -D tablet is a combination of Trypsin+Bromelain+Rutoside+Diclofenac molecules which are used for pain relief. (texasusa.in)
  • The combination of Trypsin and Bromelain are enzymes that help in increasing blood supply and make the body produce substances that eliminate pain and swelling. (texasusa.in)
  • KRITHEAL-D is the fusion of Trypsin, Bromelain, Rutoside & Diclofenac Tablets that are used to get relief from pain and inflammation. (krishlarpharma.com)
  • Trypsin, Bromelain, Rutoside & Diclofenac Tablets work by reducing the substances that cause pain and inflammation in the body which causes pain, inflammation, and its related symptoms. (krishlarpharma.com)
  • Trypsin, Bromelain, Rutoside & Diclofenac Tablets work best when taken with food as it will help to avoid an upset stomach. (krishlarpharma.com)
  • Trypsin, Bromelain, Rutoside & Diclofenac Tablets could cause some general side effects which normally tend to go away with time but if they don't then let the doctor know about them immediately. (krishlarpharma.com)
  • Our firm is conceived as the best Trypsin, Bromelain, Rutoside & Diclofenac Tablets manufacturer and supplier in India. (krishlarpharma.com)
  • The company also offers Trypsin, Bromelain, Rutoside & Diclofenac Tablets PCD Pharma Franchise with exclusive and complete monopoly rights. (krishlarpharma.com)
  • For mass spectrometry sequence analysis, we recommend our ultra-pure MSG-Trypsin ™ that is specifically designed for mass spectrometry. (gbiosciences.com)
  • This mass spectrometry grade trypsin is methylated, TPCK treated, and affinity purified. (emdmillipore.com)
  • The EDTA concentration in Trypsin EDTA Solution A (0.25%), EDTA (0.02%) is 0.53 mM. (bioind.com)
  • TPCK-trypsin helps the virus to infect the cell through cleaving the HA protein into HA1 and HA2. (cram.com)
  • According to Lee et al the optimum TPCK-trypsin concentration that can be used to infect DF-1 cells with IAV is 0.1 mg/ml (Lee et al. (cram.com)
  • I am planning to try different concentrations of TPCK-trypsin to see which concentration will work better in order not to lose cells as well as helping the IAV to infect them. (cram.com)
  • Ancordin, the major rhizome protein of madeira-vine, with trypsin inhibitory and stimulatory activities in nitric oxide productions Peptides. (moleculardepot.com)
  • The catalytic activity of the serine proteases from the trypsin family is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a histidine, which itself is hydrogen-bonded to a serine. (embl.de)
  • A partial list of proteases known to belong to the trypsin family is shown below. (embl.de)
  • In this study, we demonstrated that the host proteases TMPRSS2 and TMPRSS11D mediate the trypsin -independent infection and growth of RVA. (bvsalud.org)
  • Trypsin cuts peptide chains mainly at the carboxyl side of the amino acids lysine or arginine. (wikipedia.org)
  • Prepare Digestion Solution: add 200 µl 50 mM Ammonium Bicarbonate Solution (provided with FASP Kit) to 20 µg Trypsin-ultra ( NEB #P8101 ). (neb.com)
  • For protein quantities less than 25 µg, use 5-10 µg Trypsin-ultra and add 50 mM Ammonium Bicarbonate to bring total Digestion Solution volume to 100 µl. (neb.com)
  • The effects of UV-C light irradiation and low-temperature long-time (LTLT) pasteurization on protein structural changes, degree of hydrolysis (DH) by trypsin, peptide profile of tryptic hydrolysates by MALDI-TOF/TOF-MS, and bioavailability of β-lactoglobulin were compared. (ku.dk)
  • Compared with native or LTLT pasteurised samples, the hydrolysis rate constant of β-lactoglobulin treated with UV-C increased significantly, implying that the protein backbone cleavage sites became more accessible, whereas thermal treatment produced aggregates that impede trypsin activity. (ku.dk)
  • Trypsin - plasma or serum. (nih.gov)
  • Description: A sandwich ELISA kit for detection of Trypsin from Pig in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (orbitalbiosciences.com)
  • Description: Quantitative sandwich ELISA for measuring Pig Trypsin (TRY) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids. (orbitalbiosciences.com)
  • Description: This is Double-antibody Sandwich Chemiluminescent immunoassay for detection of Pig Trypsin (TRY) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids. (orbitalbiosciences.com)
  • Total trypsin inhibition in New Zealand pea cultivars was found to be negatively correlated to tannin content. (lincoln.ac.nz)
  • Thus it appears that the presence of tannins does not contribute to trypsin inhibition. (lincoln.ac.nz)
  • Lytic effect of trypsin, lysozyme, and complement on Treponema pallidum. (bmj.com)
  • Trypsin is considered an endopeptidase, i.e., the cleavage occurs within the polypeptide chain rather than at the terminal amino acids located at the ends of polypeptides. (wikipedia.org)
  • Trypsin should be stored at very cold temperatures (between −20 and −80 °C) to prevent autolysis, which may also be impeded by storage of trypsin at pH 3 or by using trypsin modified by reductive methylation. (wikipedia.org)
  • A chemically modified trypsin that is resistant to autolysis and degradation. (emdmillipore.com)
  • Trypsin has effective uses in foods and pharmaceuticals, as well as in tissue dissociation, cell harvesting, and microbiological media. (bioseutica.com)
  • To a 20 g vial of lyophilized trypsin add 2ml of 25 mM ammonium bicarbonate, pH 8.0. (biosyn.com)
  • Trypsin solutions are widely utilized as cell dissociation reagents for continuous cell culture of adherent growing cells. (bioind.com)
  • If the gel was SYPRO or silver-stained, use ammonium bicarbonate buffer only to maintain the trypsin level. (biosyn.com)
  • Trypsin isoinhibitors for ten of the cultivars were extracted using hydrochloric acid and purified by size exclusion chromatography and anion exchange chromatography. (lincoln.ac.nz)
  • Because TMPRSS2 and TMPRSS11D gene expression induced similar or higher levels of RVA growth as trypsin -supplemented culture , this approach offers potential advantages for RVA research and development . (bvsalud.org)
  • TRYPSIN II is ideally suited for functional food and food processing applications. (bioseutica.com)
  • 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 well as trypsin Y with a range of 2 to 30 °C (36 to 86 °F) and a maximal activity at 21 °C (70 °F). As a protein, trypsin has various molecular weights depending on the source. (wikipedia.org)
  • With the FASP kit a higher trypsin concentration is suggested. (neb.com)