A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.
A genus of leguminous shrubs or trees, mainly tropical, yielding useful compounds such as ALKALOIDS and PLANT LECTINS.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
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.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.
A low-molecular-weight protein (minimum molecular weight 8000) which has the ability to inhibit trypsin as well as chymotrypsin at independent binding sites. It is characterized by a high cystine content and the absence of glycine.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The sum of the weight of all the atoms in a molecule.
A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The rate dynamics in chemical or physical systems.
A heterogeneous mixture of glycoproteins responsible for the gel structure of egg white. It has trypsin-inhibiting activity.
The inactive proenzyme of trypsin secreted by the pancreas, activated in the duodenum via cleavage by enteropeptidase. (Stedman, 25th ed)
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995)
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
The process of cleaving a chemical compound by the addition of a molecule of water.
Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.
A high-molecular-weight protein (approximately 22,500) containing 198 amino acid residues. It is a strong inhibitor of trypsin and human plasmin.
Tests based on the biochemistry and physiology of the exocrine pancreas and involving analysis of blood, duodenal contents, feces, or urine for products of pancreatic secretion.
A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.
Glycoprotein found in alpha(1)-globulin region in human serum. It inhibits chymotrypsin-like proteinases in vivo and has cytotoxic killer-cell activity in vitro. The protein also has a role as an acute-phase protein and is active in the control of immunologic and inflammatory processes, and as a tumor marker. It is a member of the serpin superfamily.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A group of amylolytic enzymes that cleave starch, glycogen, and related alpha-1,4-glucans. (Stedman, 25th ed) EC 3.2.1.-.
Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC 3.4.2.1 and EC 3.4.12.2.
A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
Glycoproteins with a molecular weight of approximately 620,000 to 680,000. Precipitation by electrophoresis is in the alpha region. They include alpha 1-macroglobulins and alpha 2-macroglobulins. These proteins exhibit trypsin-, chymotrypsin-, thrombin-, and plasmin-binding activity and function as hormonal transporters.
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
An actinomycete from which the antibiotics STREPTOMYCIN, grisein, and CANDICIDIN are obtained.
A malabsorption condition resulting from greater than 10% reduction in the secretion of pancreatic digestive enzymes (LIPASE; PROTEASES; and AMYLASE) by the EXOCRINE PANCREAS into the DUODENUM. This condition is often associated with CYSTIC FIBROSIS and with chronic PANCREATITIS.
A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. This family includes alpha 1-antitrypsin, angiotensinogen, ovalbumin, antiplasmin, alpha 1-antichymotrypsin, thyroxine-binding protein, complement 1 inactivators, antithrombin III, heparin cofactor II, plasminogen inactivators, gene Y protein, placental plasminogen activator inhibitor, and barley Z protein. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known.
The fluid containing digestive enzymes secreted by the pancreas in response to food in the duodenum.
An enzyme that catalyzes the hydrolysis of proteins, including elastin. It cleaves preferentially bonds at the carboxyl side of Ala and Val, with greater specificity for Ala. EC 3.4.21.37.
A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.
Fluids originating from the epithelial lining of the intestines, adjoining exocrine glands and from organs such as the liver, which empty into the cavity of the intestines.
A family of unenveloped RNA viruses with cubic symmetry. The twelve genera include ORTHOREOVIRUS; ORBIVIRUS; COLTIVIRUS; ROTAVIRUS; Aquareovirus, Cypovirus, Phytoreovirus, Fijivirus, Seadornavirus, Idnoreovirus, Mycoreovirus, and Oryzavirus.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
The encapsulated embryos of flowering plants. They are used as is or for animal feed because of the high content of concentrated nutrients like starches, proteins, and fats. Rapeseed, cottonseed, and sunflower seed are also produced for the oils (fats) they yield.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Benzoic acid esters or salts substituted with one or more iodine atoms.
Proteins prepared by recombinant DNA technology.
Plants whose roots, leaves, seeds, bark, or other constituent parts possess therapeutic, tonic, purgative, curative or other pharmacologic attributes, when administered to man or animals.
A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction or the lysis of fibrin and quickly inactivated by antiplasmins.
Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A proteolytic enzyme obtained from Streptomyces griseus.
Physiologically inactive substances that can be converted to active enzymes.
Electrophoresis in which paper is used as the diffusion medium. This technique is confined almost entirely to separations of small molecules such as amino acids, peptides, and nucleotides, and relatively high voltages are nearly always used.
A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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.

Trypsin inhibitors are substances that inhibit the activity of trypsin, an enzyme that helps digest proteins in the small intestine. Trypsin inhibitors can be found in various foods such as soybeans, corn, and raw egg whites. In the case of soybeans, trypsin inhibitors are denatured and inactivated during cooking and processing.

In a medical context, trypsin inhibitors may be used therapeutically to regulate excessive trypsin activity in certain conditions such as pancreatitis, where there is inflammation of the pancreas leading to the release of activated digestive enzymes, including trypsin, into the pancreas and surrounding tissues. By inhibiting trypsin activity, these inhibitors can help reduce tissue damage and inflammation.

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.

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.

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.

'Erythrina' is a botanical term, not a medical one. It refers to a genus of plants in the family Fabaceae, also known as the pea or legume family. These plants are commonly called coral trees due to their bright red flowers. While some parts of certain species can have medicinal uses, such as anti-inflammatory and analgesic properties, 'Erythrina' itself is not a medical term or condition.

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).

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.

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.

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.

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.

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.

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.

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.

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.

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.

Cathepsin G is a serine protease, which is a type of enzyme that breaks down other proteins. It is produced and released by neutrophils, a type of white blood cell that plays an important role in the body's immune response to infection. Cathepsin G helps to digest and kill microorganisms that have invaded the body. It can also contribute to tissue damage and inflammation in certain diseases, such as rheumatoid arthritis and cystic fibrosis.

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.

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.

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.

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.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

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.

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.

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).

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.

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.

"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.

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.

"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.

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.

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.

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.

Pancreatic function tests are a group of medical tests that are used to assess the functionality and health of the pancreas. The pancreas is a vital organ located in the abdomen, which has two main functions: an exocrine function, where it releases digestive enzymes into the small intestine to help break down food; and an endocrine function, where it produces hormones such as insulin and glucagon that regulate blood sugar levels.

Pancreatic function tests typically involve measuring the levels of digestive enzymes in the blood or stool, or assessing the body's ability to digest and absorb certain nutrients. Some common pancreatic function tests include:

1. Serum amylase and lipase tests: These tests measure the levels of digestive enzymes called amylase and lipase in the blood. Elevated levels of these enzymes may indicate pancreatitis or other conditions affecting the pancreas.
2. Fecal elastase test: This test measures the level of elastase, an enzyme produced by the pancreas, in a stool sample. Low levels of elastase may indicate exocrine pancreatic insufficiency (EPI), a condition where the pancreas is not producing enough digestive enzymes.
3. Secretin stimulation test: This test involves administering a medication called secretin, which stimulates the pancreas to release digestive enzymes. The levels of these enzymes are then measured in the blood or duodenum (the first part of the small intestine).
4. Fat absorption tests: These tests involve measuring the amount of fat that is absorbed from a meal. High levels of fat in the stool may indicate EPI.
5. Glucose tolerance test: This test involves measuring blood sugar levels after consuming a sugary drink. Low levels of insulin or high levels of glucose may indicate diabetes or other endocrine disorders affecting the pancreas.

Overall, pancreatic function tests are important tools for diagnosing and monitoring conditions that affect the pancreas, such as pancreatitis, EPI, and diabetes.

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.

Alpha 1-Antichymotrypsin (ACT), also known as Serpin A1, is a protein found in the blood that belongs to the serine protease inhibitor family. It functions to regulate enzymes that break down other proteins in the body. ACT helps to prevent excessive and potentially harmful proteolytic activity, which can contribute to tissue damage and inflammation.

Deficiency or dysfunction of alpha 1-Antichymotrypsin has been associated with several medical conditions, including:

1. Alpha 1-Antichymotrypsin Deficiency: A rare genetic disorder characterized by low levels of ACT in the blood, which can lead to increased risk of developing lung and liver diseases.
2. Alzheimer's Disease: Increased levels of ACT have been found in the brains of individuals with Alzheimer's disease, suggesting a possible role in the pathogenesis of this neurodegenerative disorder.
3. Cancer: Elevated levels of ACT have been observed in various types of cancer, including lung, breast, and prostate cancers, potentially contributing to tumor growth and metastasis.
4. Inflammatory and immune-mediated disorders: Increased ACT levels are associated with several inflammatory conditions, such as rheumatoid arthritis, systemic lupus erythematosus (SLE), and vasculitis, suggesting its involvement in the regulation of the immune response.
5. Cardiovascular diseases: Elevated ACT levels have been linked to an increased risk of developing cardiovascular diseases, including atherosclerosis and myocardial infarction (heart attack).

Understanding the role of alpha 1-Antichymotrypsin in various physiological and pathological processes can provide valuable insights into disease mechanisms and potential therapeutic targets.

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.

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.

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.

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.

Subtilisins are a group of serine proteases that are produced by certain bacteria, including Bacillus subtilis. They are named after the bacterium and the Latin word "subtilis," which means delicate or finely made. Subtilisins are alkaline proteases, meaning they work best in slightly basic conditions.

Subtilisins have a broad specificity for cleaving peptide bonds and can hydrolyze a wide range of protein substrates. They are widely used in industry for various applications such as detergents, food processing, leather treatment, and biotechnology due to their ability to function at high temperatures and in the presence of denaturing agents.

In medicine, subtilisins have been studied for their potential use in therapeutic applications, including as anti-inflammatory agents and in wound healing. However, more research is needed to fully understand their mechanisms of action and potential benefits.

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.

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.

Cathepsins are a type of proteolytic enzymes, which are found in lysosomes and are responsible for breaking down proteins inside the cell. They are classified as papain-like cysteine proteases and play important roles in various physiological processes, including tissue remodeling, antigen presentation, and apoptosis (programmed cell death). There are several different types of cathepsins, including cathepsin B, C, D, F, H, K, L, S, V, and X/Z, each with distinct substrate specificities and functions.

Dysregulation of cathepsins has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. For example, overexpression or hyperactivation of certain cathepsins has been shown to contribute to tumor invasion and metastasis, while their inhibition has been explored as a potential therapeutic strategy in cancer treatment. Similarly, abnormal levels of cathepsins have been linked to the progression of neurodegenerative diseases like Alzheimer's and Parkinson's, making them attractive targets for drug development.

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.

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.

"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.

Exocrine pancreatic insufficiency (EPI) is a condition characterized by the reduced ability to digest and absorb nutrients due to a lack of digestive enzymes produced by the exocrine glands in the pancreas. These enzymes, including lipases, amylases, and proteases, are necessary for breaking down fats, carbohydrates, and proteins in food during the digestion process.

When EPI occurs, undigested food passes through the gastrointestinal tract, leading to malabsorption of nutrients, which can result in various symptoms such as abdominal pain, bloating, diarrhea, weight loss, and steatorrhea (fatty stools). EPI is often associated with chronic pancreatitis, cystic fibrosis, pancreatic cancer, or other conditions that damage the exocrine glands in the pancreas.

EPI can be diagnosed through various tests, including fecal elastase testing, fecal fat quantification, and imaging studies to assess the structure and function of the pancreas. Treatment typically involves replacing the missing enzymes with oral supplements taken with meals and snacks to improve digestion and absorption of nutrients. In addition, dietary modifications and management of underlying conditions are essential for optimal outcomes.

SERPINs are an acronym for "serine protease inhibitors." They are a group of proteins that inhibit serine proteases, which are enzymes that cut other proteins. SERPINs are found in various tissues and body fluids, including blood, and play important roles in regulating biological processes such as inflammation, blood clotting, and cell death. They do this by forming covalent complexes with their target proteases, thereby preventing them from carrying out their proteolytic activities. Mutations in SERPIN genes have been associated with several genetic disorders, including emphysema, cirrhosis, and dementia.

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.

Leukocyte elastase is a type of enzyme that is released by white blood cells (leukocytes), specifically neutrophils, during inflammation. Its primary function is to help fight infection by breaking down the proteins in bacteria and viruses. However, if not properly regulated, leukocyte elastase can also damage surrounding tissues, contributing to the progression of various diseases such as chronic obstructive pulmonary disease (COPD), acute respiratory distress syndrome (ARDS), and cystic fibrosis.

Leukocyte elastase is often measured in clinical settings as a marker of inflammation and neutrophil activation, particularly in patients with lung diseases. Inhibitors of leukocyte elastase have been developed as potential therapeutic agents for these conditions.

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.

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.

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.

Reoviridae is a family of double-stranded RNA viruses that are non-enveloped and have a segmented genome. The name "Reoviridae" is derived from Respiratory Enteric Orphan virus, as these viruses were initially discovered in respiratory and enteric (gastrointestinal) samples but did not appear to cause any specific diseases.

The family Reoviridae includes several important human pathogens such as rotaviruses, which are a major cause of severe diarrhea in young children worldwide, and orthoreoviruses, which can cause respiratory and systemic infections in humans. Additionally, many Reoviridae viruses infect animals, including birds, mammals, fish, and insects, and can cause a variety of diseases.

Reoviridae virions are typically composed of multiple protein layers that encase the genomic RNA segments. The family is divided into two subfamilies, Sedoreovirinae and Spinareovirinae, based on structural features and genome organization. Reoviruses have a complex replication cycle that involves multiple steps, including attachment to host cells, uncoating of the viral particle, transcription of the genomic RNA, translation of viral proteins, packaging of new virions, and release from infected cells.

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.

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.

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.

Iodobenzoates are organic compounds that consist of a benzoic acid molecule with an iodine atom substituted at the carboxyl group. Specifically, an iodobenzoate is an ester derived from benzoic acid and iodine, in which the hydrogen atom of the carboxylic acid group (-COOH) has been replaced by an iodine atom.

The general formula for an iodobenzoate can be represented as C6H4(IO)CO2R, where R represents an alkyl or aryl group. Iodobenzoates have various applications in organic synthesis and pharmaceuticals, including the production of dyes, drugs, and other chemical intermediates.

It's worth noting that iodobenzoates are not a medical condition or diagnosis but rather a class of chemical compounds with potential uses in medical research and therapeutics.

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.

Medicinal plants are defined as those plants that contain naturally occurring chemical compounds which can be used for therapeutic purposes, either directly or indirectly. These plants have been used for centuries in various traditional systems of medicine, such as Ayurveda, Chinese medicine, and Native American medicine, to prevent or treat various health conditions.

Medicinal plants contain a wide variety of bioactive compounds, including alkaloids, flavonoids, tannins, terpenes, and saponins, among others. These compounds have been found to possess various pharmacological properties, such as anti-inflammatory, analgesic, antimicrobial, antioxidant, and anticancer activities.

Medicinal plants can be used in various forms, including whole plant material, extracts, essential oils, and isolated compounds. They can be administered through different routes, such as oral, topical, or respiratory, depending on the desired therapeutic effect.

It is important to note that while medicinal plants have been used safely and effectively for centuries, they should be used with caution and under the guidance of a healthcare professional. Some medicinal plants can interact with prescription medications or have adverse effects if used inappropriately.

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.

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.

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.

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.

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.

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.

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.

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.

Paper electrophoresis is a laboratory technique used to separate and analyze mixtures of charged particles, such as proteins or nucleic acids (DNA or RNA), based on their differing rates of migration in an electric field. In this method, the sample is applied to a strip of paper, usually made of cellulose, which is then placed in a bath of electrophoresis buffer.

An electric current is applied across the bath, creating an electric field that causes the charged particles in the sample to migrate along the length of the paper. The rate of migration depends on the charge and size of the particle: more highly charged particles move faster, while larger particles move more slowly. This allows for the separation of the individual components of the mixture based on their electrophoretic mobility.

After the electrophoresis is complete, the separated components can be visualized using various staining techniques, such as protein stains for proteins or dyes specific to nucleic acids. The resulting pattern of bands can then be analyzed to identify and quantify the individual components in the mixture.

Paper electrophoresis has been largely replaced by other methods, such as slab gel electrophoresis, due to its lower resolution and limited separation capabilities. However, it is still used in some applications where a simple, rapid, and low-cost method is desired.

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.

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.

... (EC 3.4.21.1, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, ... Wilcox PE (1970). "[5] Chymotrypsinogens-chymotrypsins". Chymotrypsinogens - chymotrypsins. Methods in Enzymology. Vol. 19. pp ... producing α-chymotrypsin (which is more active and stable than π-chymotrypsin). The resulting molecule is a three-polypeptide ... alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the ...
Chymotrypsin C, also known as caldecrin or elastase 4, is an enzyme that in humans is encoded by the CTRC gene. Chymotrypsin C ... Brecher AS, Yang MP (1998). "Acetaldehyde inhibits chymotrypsin and serum anti-chymotrypsin activity". J. Investig. Med. 46 (4 ... "Entrez Gene: chymotrypsin C (caldecrin)". Tomomura A, Akiyama M, Itoh H, Yoshino I, Tomomura M, Nishii Y, Noikura T, Saheki T ( ... 2008). "Chymotrypsin C (CTRC) alterations that diminish activity or secretion are associated with chronic pancreatitis". Nat. ...
Chymotrypsin+C at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.21). ... Chymotrypsin C (EC 3.4.21.2) is an enzyme. This enzyme catalyses the following chemical reaction: Preferential cleavage: Leu-, ... Folk, J.E. (1970). "Chymotrypsin C (porcine pancreas)". Methods Enzymol. Methods in Enzymology. 19: 109-112. doi:10.1016/0076- ... Wilcox PE (1970). "Chymotrypsinogens - chymotrypsins". Methods Enzymol. Methods in Enzymology. 19: 64-108. doi:10.1016/0076- ...
More generally, he made a study of mechanisms for chymotrypsin catalysis., and in particular the "charge-relay" system as a way ... Bruice, T. C. (1961). "The Mechanisms for Chymotrypsin". Proceedings of the National Academy of Sciences. 47 (12): 1924-1928. ...
When he moved to the University of Cambridge, she joined him, and studied the chymotrypsin inhibitor 2 (CI2). In Cambridge ... Sophie E. Jackson; Alan R. Fersht (1 October 1991). "Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state ... "Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2". Biochemistry. 32 (42): 11259-69. doi: ...
Tabushi I, Yamada H, Matsuzaki H, Furukawa J (August 1975). "Polyester readily hydrolyzable by chymotrypsin". Journal of ... in the case of α-chymotrypsin) and 1977 (lipase). PET plastic came into widespread use in the 1970s and it has been suggested ...
Chymotrypsin-like protease CTRL-1 is an enzyme that in humans is encoded by the CTRL gene. GRCh38: Ensembl release 89: ... "Entrez Gene: CTRL chymotrypsin-like". Human CTRL genome location and CTRL gene details page in the UCSC Genome Browser. ... Heidtmann HH, Travis J (1994). "A novel chymotrypsin-like serine proteinase from human lung". Biol. Chem. Hoppe-Seyler. 374 (9 ... 1997). "A novel human chymotrypsin-like digestive enzyme". J. Biol. Chem. 272 (12): 8099-104. doi:10.1074/jbc.272.12.8099. PMID ...
Chymotrypsin-like elastase family member 2B is and enzyme that in humans is encoded by the CELA2B gene. Elastases form a ... "Entrez Gene: chymotrypsin-like elastase family". Human CELA2B genome location and CELA2B gene details page in the UCSC Genome ...
Early in his career, Knowles studied α-chymotrypsin and pepsin, which are nonspecific proteases, meaning they accept a broad ... Ingles, DW; Knowles, JR (1967). "Specificity and stereospecificity of α-chymotrypsin". Biochemical Journal. 104 (2): 369-377. ...
Trypsin- and chymotrypsin-inhibitor from soybeans". International Journal of Peptide and Protein Research. 25 (2): 113-31. doi: ...
Gutfreund, H.; Sturtevant, J. M. (1956). "The Mechanism of Chymotrypsin-Catalyzed Reactions". Proceedings of the National ... including chymotrypsin and trypsin, and was especially active in using methods of studying fast reactions to study enzyme ...
1. Chymotrypsin Catalyzed Hydrolysis of p-Nitroanilides of Phenylalanine and Tyrosine Attached to Side-Chains of Copolymers of ... 6. Hydrophilic Gels Cleavable by Chymotrypsin". Biomaterials 3, 150-154 (1982) J. Kopeček, P. Rejmanová, V. Chytrý, "Polymers ...
Hartley, BS; V Massey (1956). "The active center of chymotrypsin: 1. Labelling with a fluorescent dye". Biochimica et ...
It inhibits proteases like chymotrypsin, kallikrein, plasmin, thrombin, and trypsin. The specificity is similar to the ... Formation and Reactions of Phenylmethanesulfonyl α-Chymotrypsin". Biochemistry. 3 (6): 783-791. doi:10.1021/bi00894a009. PMID ...
Chymotrypsin, trypsin and Diclofenac are also recommended. "Osteoarthritis". The Lecturio Medical Concept Library. Retrieved 27 ...
Bernal JD, Fankuchen I, Perutz M (1938). "X-ray study of chymotrypsin and hemoglobin". Nature. 141: 523-524. doi:10.1038/ ... The early crystal structures included chymotrypsin (PDB file 2CHA), chymotrypsinogen (PDB file 1CHG), trypsin (PDB file 1PTN), ... Matthews BW, Sigler PB, Henderson R, Blow DM (1967). "Three-dimensional structure of tosyl-α-chymotrypsin". Nature. 214 (5089 ... comparison with α-chymotrypsin, and implications for zymogen activation". Biochemistry. 9 (9): 1997-2009. doi:10.1021/ ...
TPCK is an irreversible inhibitor of chymotrypsin. Also inhibits some cysteine proteases such as caspase, papain, bromelain or ... as in chymotrypsin, in which it binds to the Histidine-57 residue in the active site). TPCK-treated trypsin is used to improve ...
Fersht AR, Sperling J (February 1973). "The charge relay system in chymotrypsin and chymotrypsinogen". J. Mol. Biol. 74 (2): ...
Postoperative ocular hypertension from use of alpha chymotrypsin. Glaucoma of miscellaneous origin Associated with intraocular ... Drug-induced glaucoma Corticosteroid induced glaucoma Alpha-chymotrypsin glaucoma. ...
Some SSI's also inhibit trypsin, chymotrypsin and griselysin. Commercially, SSI's have huge potential in the commercial market ...
Chymotrypsin-like elastase family member 3B also known as elastase-3B, protease E, or fecal elastase is an enzyme that in ... September 2004). "Fecal chymotrypsin and elastase-1 determination on one single stool collected at random: diagnostic value for ... chymotrypsin and kallikrein, it has a digestive function in the intestine. Elastase 3B preferentially cleaves proteins after ... literature that describes human elastase 1 activity in the pancreas or fecal material is actually referring to chymotrypsin- ...
They inhibit chymotrypsin, a peptidase belong to the S1 family (INTERPRO). Rawlings ND, Tolle DP, Barrett AJ (2004). " ... Pacifastin inhibits the serine peptidases trypsin and chymotrypsin. All pacifastin members that have been characterized at the ...
Bernal, J. D.; Fankuchen, I.; Perutz, MAX (1938). "An X-Ray Study of Chymotrypsin and Haemoglobin". Nature. 141 (3568): 523-524 ... Bernal during which time they examined the structure of chymotrypsin and haemoglobin. He also collaborated with Bernal's ...
Bender, Myron L.; Zerner, Burt (1961). "The formation of the acyl-enzyme intermediate, trans-cinnamoyl-α-chymotrypsin, in the ... Kezdy, Ferenc J.; Bender, Myron L. (1962). "The Kinetics of the α-Chymotrypsin-Catalyzed Hydrolysis of p-Nitrophenyl Acetate". ... Brot, Frederick E.; Bender, Myron L. (1969). "Use of the specificity constant of α-chymotrypsin". Journal of the American ... Philipp, Manfred; Bender, Myron L. (1973). "Is binding the rate-limiting step in acylation of alpha-chymotrypsin by specific ...
The enzymes trypsin and chymotrypsin were first purified in the 1930s. A serine in each of trypsin and chymotrypsin was ... The structure of chymotrypsin was solved by X-ray crystallography in the 1960s, showing the orientation of the catalytic triad ... Blow DM, Birktoft JJ, Hartley BS (1969). "Role of a buried acid group in the mechanism of action of chymotrypsin". Nature. 221 ... The triad is exemplified by chymotrypsin, a model serine protease from the PA superfamily which uses its triad to hydrolyse ...
Genetically engineered mutants of the chymotrypsin serine protease were shown to have some proteinase activity even though ... McLachlan AD (February 1979). "Gene duplications in the structural evolution of chymotrypsin". Journal of Molecular Biology. ...
This mechanism is utilised by the catalytic triad of enzymes such as proteases like chymotrypsin and trypsin, where an acyl- ... For example, the energetics of the covalent bond to the serine molecule in chymotrypsin should be compared to the well- ... Fersht AR, Requena Y (December 1971). "Mechanism of the -chymotrypsin-catalyzed hydrolysis of amides. pH dependence of k c and ... Consider the reaction of peptide bond hydrolysis catalyzed by a pure protein α-chymotrypsin (an enzyme acting without a ...
Additionally, trypsin inhibitor partially interferes with chymotrypsin function. Trypsinogen is an inactive form of trypsin, ... is formed in the pancreas and activated to trypsin with enteropeptidase Chymotrypsinogen is the inactive form of chymotrypsin ...
Purification and properties, and formation of pi-chymotrypsin". The Biochemical Journal. 147 (1): 45-53. doi:10.1042/bj1470045 ...
Stevenson KJ, Gibson D, Dixon GH (February 1974). "Amino acid analyses of chymotrypsin-like proteases from the sea anemone ( ... Gibson D, Dixon GH (May 1969). "Chymotrypsin-like proteases from the sea anemone, Metridium senile". Nature. 222 (5195): 753-6 ...
Chymotrypsin (EC 3.4.21.1, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, ... Wilcox PE (1970). "[5] Chymotrypsinogens-chymotrypsins". Chymotrypsinogens - chymotrypsins. Methods in Enzymology. Vol. 19. pp ... producing α-chymotrypsin (which is more active and stable than π-chymotrypsin). The resulting molecule is a three-polypeptide ... alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the ...
When the pancreas does not produce enough trypsin and chymotrypsin, smaller-than-normal amounts can be seen in ... Trypsin and chymotrypsin are substances released from the pancreas during normal digestion. ... Trypsin and chymotrypsin are substances released from the pancreas during normal digestion. When the pancreas does not produce ... An abnormal result means the trypsin or chymotrypsin levels in your stool are below the normal range. This may mean that your ...
J:7529 Honey NK, et al., Chromosomal assignments of genes for trypsin, chymotrypsin B, and elastase in mouse. Somat Cell Mol ...
If the file Chymotrypsin needs to be in a different folder, then specify the exact path, e.g., "SETUP=C:/my files/Chymotrypsin ... Line 1: SETUP=chymotrypsin.txt site=(F16(+),G194(-),F102(-)). Line 2: PDB Chymotrypsin, ionizing the residues 16, 102, and 194 ... Line 1: SETUP=chymotrypsin.txt Line 2: PDB Chymotrypsin, ionizing the residues 16, 102, and 194. Line 3: ... In the PDB file, this system is described as "GAMMA-CHYMOTRYPSIN IS A COMPLEX OF ALPHA-CHYMOTRYPSIN WITH ITS OWN. TITLE 2 ...
A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains on carboxyl end of the bond Shop MP Biomedicals™ alpha-Chymotrypsin
Biocatalytic kinetic effect of α-chymotrypsin enzyme has been investigated in its free and pretreated forms (it was covered by ... in Section 3.1). KM value of pretreated α-chymotrypsin enzyme as NP2 (KM = 1.4 mM) is a little bit higher than that of KM value ... KM constant of immobilized α-chymotrypsin enzyme (NP2) has more or less the same value (1.4 mM) than that of free E (1.2 mM) ( ... Surprisingly, KM value of the α-chymotrypsin enzyme nanoparticles (NP2) is about 1.17 times as much as KM value of free enzyme ...
Submit a product review for Recombinant Human Chymotrypsin C/CTRC Protein, CF 6907-SE-010 ... Home » Chymotrypsin C/CTRC » Recombinant Human Chymotrypsin C/CTRC Protein, CF » Submit a Review ...
Alpha-Chymotrypsin Posted on December 26, 2011 by Life What is Alpha-Chymotrypsin? Alpha-Chymotrypsin is a specific digestive ... acid alpha Amylase bacteria beans beneficial betaine body burn fat cholesterol chymotrypsin complex diastase digestion ... Posted in , Tagged alpha, chymotrypsin, digestion, digestive, Enzymes, proteins , Leave a comment ...
The α-chymotrypsin-catalyzed hydrolyses of a number of N-acetylated dipeptide methyl esters were studied. The results are ... A series of N-acetylated peptide esters of varying length have been evaluated as substrates of α-chymotrypsin. The results are ... Finally, some reactive esters of N-acetylated amino acids have been evaluated as substrates of α-chymotrypsin. Their reactivity ... Neil, Gary Lawrence (1966) The structure specificity of alpha-chymotrypsin. I. Polypeptides as substrates. II. N-acylated ...
The equilibrium and kinetics of folding of the single-domain protein chymotrypsin inhibitor 2 conform to the simple two-state ... Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for ...
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 ...
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To determine the chymotrypsin-like protease activity, Chymotrypsin-like Cell-Based Assays (Promega, Madison, WI) were used ... Measurement of chymotrypsin-like proteasome activity. To determine the changes of the levels of proteasome activity in iHTM ... We also investigated the chymotrypsin-like proteasome activity of the 20S proteasome, which was reported to protect eukaryotic ... Reactive oxygen species (ROS) levels were determined using dihydrodichlorofluorescein staining, and the chymotrypsin-like ...
CHEMISTRY OF CAGED ENZYMES /II$. PHOTOACTIVATION OF INHIBITED CHYMOTRYPSIN Coordinates. PDB Format Method. X-RAY DIFFRACTION ... Stoddard, B.L. et al., Photolysis and deacylation of inhibited chymotrypsin. Biochemistry (1990) Release Date. 1990-10-15. ... GAMMA-CHYMOTRYPSIN A: AD. GAMMA-CHYMOTRYPSIN A: BE. GAMMA-CHYMOTRYPSIN A: CF. SMTL:PDB. SMTL Chain Id:. PDB Chain Id:. A. E ...
North America Chymotrypsin Market Report (2014-2024) - Market Size, Share, Price, Trend and Forecast includes market share, ... The Chymotrypsin market in North America is segmented by countries: * US * Canada * Mexico The reports analysis Chymotrypsin ... Table of Contents Table of Contents Chapter One Chymotrypsin Overview 1.1 Chymotrypsin Outline 1.2 Classification and ... of Chymotrypsin Table Application of Chymotrypsin Figure Porter Five Forces Model Analysis of North America Chymotrypsin Figure ...
THE X-RAY CRYSTAL STRUCTURE OF N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN ... A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE OF N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN ... GAMMA-CHYMOTRYPSIN A: AD. GAMMA-CHYMOTRYPSIN A: BE. GAMMA-CHYMOTRYPSIN A: CF. SMTL:PDB. SMTL Chain Id:. PDB Chain Id:. A. E ...
Chymotrypsin. An enzyme secreted by the pancreas into the small intestine to assist in protein breakdown. ... The absence or significant decrease of the pancreatic enzymes, amylase, lipase, trypsin, and chymotrypsin limits fat protein ... The absence or significant decrease of the pancreatic enzymes, amylase, lipase, trypsin, and chymotrypsin limits fat protein ...
CHYMOTRYPSIN INHIBITOR 2. A [auth I]. 83. Hordeum vulgare. Mutation(s): 0 ... Chymotrypsin inhibitor 2 (CI-2), a serine proteinase inhibitor from barley seeds, has been crystallized and its three- ...
Reverse micelles as a water-property-control system to investigate the hydration/activity relationship of a-chymotrypsin. ... Reverse micelles as a water-property-control system to investigate the hydration/activity relationship of a-chymotrypsin. / ... Reverse micelles as a water-property-control system to investigate the hydration/activity relationship of a-chymotrypsin.. ... T1 - Reverse micelles as a water-property-control system to investigate the hydration/activity relationship of a-chymotrypsin. ...
... in free adipocytes obtained by treating Sarcophaga larval fat bodies with chymotrypsin. / Okuyama, Hajime; Kurata, Shoichiro; ... in free adipocytes obtained by treating Sarcophaga larval fat bodies with chymotrypsin. In: Insect Biochemistry and Molecular ... in free adipocytes obtained by treating Sarcophaga larval fat bodies with chymotrypsin. Insect Biochemistry and Molecular ... in free adipocytes obtained by treating Sarcophaga larval fat bodies with chymotrypsin, Insect Biochemistry and Molecular ...
  • The equilibrium and kinetics of folding of the single-domain protein chymotrypsin inhibitor 2 conform to the simple two-state model. (au.dk)
  • 3: Wilimowska-Pelc A, Olichwier Z, Mazurkiewicz A, Kowalska J, Wilusz T. Kazal-type chymotrypsin inhibitor from duck pancreas Comp Biochem Physiol B Biochem Mol Biol. (moleculardepot.com)
  • Chymotrypsin inhibitor 2 (CI-2), a serine proteinase inhibitor from barley seeds, has been crystallized and its three-dimensional structure determined at 2.0-A resolution by the molecular replacement method. (rcsb.org)
  • Amino Acid Sequence of Chymotrypsin Inhibitor ECI from the Seeds of Erythrina Variegata (LINN. (elsevierpure.com)
  • The amino acids of the chymotrypsin inhibitor (ECI) from the Erythrina variegata seeds have been sequenced. (elsevierpure.com)
  • The example used here is for chymotrypsin, but the steps for other enzymes are similar. (openmopac.net)
  • The absence or significant decrease of the pancreatic enzymes , amylase, lipase , trypsin, and chymotrypsin limits fat protein and carbohydrate digestion, resulting in steatorrhea due to fat malabsorption. (digitalnaturopath.com)
  • In order to develop effective alternate substrate inhibitors for serine proteases, we have prepared a series of β-substituted β-phenylpropionic acid esters related to some systems known to form stable acyl enzymes with α-chymotrypsin. (illinois.edu)
  • Chymotrypsin is synthesized in the pancreas. (wikipedia.org)
  • Trypsin and chymotrypsin are substances released from the pancreas during normal digestion. (medlineplus.gov)
  • When the pancreas does not produce enough trypsin and chymotrypsin, smaller-than-normal amounts can be seen in a stool sample. (medlineplus.gov)
  • Catalog Number: B2014400 (5 mg) α-Chymotrypsin from Bovine Pancreas is a high quality α-Chymotrypsin purified from bovine pancreas. (moleculardepot.com)
  • The effects of digestion by bovine pancreas alpha-chymotrypsin on native bovine glutamate dehydrogenase Biochem Soc Trans. (moleculardepot.com)
  • Chymotrypsin (Chymar) is extractedfrom mammalian pancreas and is used in cataractsurgery. (leaderbio-ingredients.com)
  • We are able to gain huge popularity in the industry, by offering an exceptional range of Trypsin Chymotrypsin Tablets . (adsilaorganics.com)
  • Our Trypsin Chymotrypsin Tablets is formulated by a diligent team of medical experts using optimum grade compounds at our ultramodern machining facility. (adsilaorganics.com)
  • 2. Comparison between human urinary kallikrein and human urokinase, bovine beta-trypsin, bovine thrombin, and bovine alpha-chymotrypsin Biochemistry. (moleculardepot.com)
  • Alpha-Chymotrypsin is a specific digestive enzyme that performs proteolyisis, which is breaking down proteins from the small intestine. (worldofenzymes.info)
  • The structural specificity of α-chymotrypsin for polypeptides and denatured proteins has been examined. (caltech.edu)
  • In vivo, chymotrypsin is a proteolytic enzyme (serine protease) acting in the digestive systems of many organisms. (wikipedia.org)
  • Chymotrypsin cleaves peptide bonds by attacking the unreactive carbonyl group with a powerful nucleophile, the serine 195 residue located in the active site of the enzyme, which briefly becomes covalently bonded to the substrate, forming an enzyme-substrate intermediate. (wikipedia.org)
  • Reactive oxygen species (ROS) levels were determined using dihydrodichlorofluorescein staining, and the chymotrypsin-like protease activities were measured using the Suc-LLVY-aminoluciferin substrate. (molvis.org)
  • The main substrates of chymotrypsin are peptide bonds in which the amino acid N-terminal to the bond is a tryptophan, tyrosine, phenylalanine, or leucine. (wikipedia.org)
  • A series of N-acetylated peptide esters of varying length have been evaluated as substrates of α-chymotrypsin. (caltech.edu)
  • Finally, some reactive esters of N-acetylated amino acids have been evaluated as substrates of α-chymotrypsin. (caltech.edu)
  • Like many proteases, chymotrypsin also hydrolyses amide bonds in vitro, a virtue that enabled the use of substrate analogs such as N-acetyl-L-phenylalanine p-nitrophenyl amide for enzyme assays. (wikipedia.org)
  • The α-chymotrypsin-catalyzed hydrolyses of a number of N-acetylated dipeptide methyl esters were studied. (caltech.edu)
  • This system consists of chymotrypsin residues 1-11 and 16-245, a three-residue substrate GAW in the active site, four sulfate ions, and 346 water molecules. (openmopac.net)
  • The preparation of trypsins and chymotrypsins from bovine and porcine residues after insulin extraction Prep Biochem. (moleculardepot.com)
  • Chymotrypsin preferentially cleaves peptide amide bonds where the side chain of the amino acid N-terminal to the scissile amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). (wikipedia.org)
  • Chymotrypsin catalysis of the hydrolysis of a protein substrate (in red) is performed in two steps. (wikipedia.org)
  • Trypsin-Chymotrypsin is a white or yellowish powder having proteolytic activity. (sunwisechem.com)
  • Abstract: The North America Chymotrypsin market size is $XX million USD in 2018 with XX CAGR from 2014 to 2018, and it is expected to reach $XX million USD by the end of 2024 with a CAGR of XX% from 2019 to 2024. (marketresearchinc.com)
  • abstract = "The molecular mechanism(s) involved in the selective cessation of protein synthesis in free adipocytes obtained by treating fat bodies of Sarcophaga larvae with chymotrypsin were investigated (Okuyama, H., Kurata, S., Natori, S., 1994. (elsevierpure.com)
  • In addition to the data part, the report also provides overview of Chymotrypsin market, including classification, application, manufacturing technology, industry chain analysis and latest market dynamics. (marketresearchinc.com)
  • Acyl enzyme species were generated from chymotrypsin by reaction with the active esters, and the progress of deacylation was monitored by the proflavin displacement assay. (illinois.edu)
  • Moreover, chymotrypsin induces its own activation by cleaving in positions 14-15, 146-147, and 148-149, producing α-chymotrypsin (which is more active and stable than π-chymotrypsin). (wikipedia.org)
  • Reverse micelles as a water-property-control system to investigate the hydration/activity relationship of a-chymotrypsin. (wur.nl)
  • For this exercise, create a file "Chymotrypsin.txt" in the folder where the jobs are being run, and edit the file to insert one line: "EPS=78.4 MOZYME GNORM=10 CHARGE=-1 PDBOUT" Save the file. (openmopac.net)
  • If the file Chymotrypsin needs to be in a different folder, then specify the exact path, e.g. (openmopac.net)
  • In each data-set, add the keyword "SETUP=Chymotrypsin.txt" and delete the keywords EPS=78.4, MOZYME, GNORM=10 CHARGE=-1, if present. (openmopac.net)
  • An abnormal result means the trypsin or chymotrypsin levels in your stool are below the normal range. (medlineplus.gov)
  • If trypsin or chymotrypsin are present, the gelatin will clear. (medlineplus.gov)
  • α-Chymotrypsin from bovine has been used in a study to inform proteasome inhibition in order to advance anticancer research. (leaderbio-ingredients.com)
  • α-Chymotrypsin from bovine has also been used in a study that functionalized surface anchored poly(methylhydrosiloxane) thin films on oxidized silicon wafers. (leaderbio-ingredients.com)
  • This report is an essential reference for who looks for detailed information on North America Chymotrypsin market. (marketresearchinc.com)
  • Biocatalytic kinetic effect of α -chymotrypsin enzyme has been investigated in its free and pretreated forms (it was covered by a very thin, porous polymer layer, called enzyme nanoparticle) as well as its immobilized form into pores of polysulfone/polyamide asymmetric, hydrophilic membrane. (mdpi.com)