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.
The inactive proenzyme of trypsin secreted by the pancreas, activated in the duodenum via cleavage by enteropeptidase. (Stedman, 25th ed)
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 group of amylolytic enzymes that cleave starch, glycogen, and related alpha-1,4-glucans. (Stedman, 25th ed) EC 3.2.1.-.
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 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.
Physiologically inactive substances that can be converted to active enzymes.
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
A ZINC-dependent carboxypeptidase primary found in the DIGESTIVE SYSTEM. The enzyme catalyzes the preferential cleavage of a C-terminal peptidyl-L-lysine or arginine. It was formerly classified as EC 3.4.2.2 and EC 3.4.12.3.
A specific decapeptide obtained from the skin of Hila caerulea, an Australian amphibian. Caerulein is similar in action and composition to CHOLECYSTOKININ. It stimulates gastric, biliary, and pancreatic secretion; and certain smooth muscle. It is used in paralytic ileus and as diagnostic aid in pancreatic malfunction.
A peptide, of about 33 amino acids, secreted by the upper INTESTINAL MUCOSA and also found in the central nervous system. It causes gallbladder contraction, release of pancreatic exocrine (or digestive) enzymes, and affects other gastrointestinal functions. Cholecystokinin may be the mediator of satiety.
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.
An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. It is produced by glands on the tongue and by the pancreas and initiates the digestion of dietary fats. (From Dorland, 27th ed) EC 3.1.1.3.
A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 3.2.1.17.
A specialized proteolytic enzyme secreted by intestinal cells. It converts TRYPSINOGEN into its active form TRYPSIN by removing the N-terminal peptide. EC 3.4.21.9.
A malabsorption syndrome that is precipitated by the ingestion of foods containing GLUTEN, such as wheat, rye, and barley. It is characterized by INFLAMMATION of the SMALL INTESTINE, loss of MICROVILLI structure, failed INTESTINAL ABSORPTION, and MALNUTRITION.
A bile salt formed in the liver by conjugation of deoxycholate with glycine, usually as the sodium salt. It acts as a detergent to solubilize fats for absorption and is itself absorbed. It is used as a cholagogue and choleretic.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
The shortest and widest portion of the SMALL INTESTINE adjacent to the PYLORUS of the STOMACH. It is named for having the length equal to about the width of 12 fingers.
The simplest of all peptides. It functions as a gamma-glutamyl acceptor.

Immunoreactive pancreatic Reg protein in sera from cystic fibrosis patients with and without pancreatic insufficiency. (1/124)

BACKGROUND: The biological function of the Reg protein, a non-enzymic protein produced in fairly large amounts by pancreatic acinar cells, remains elusive. Its susceptibility to proteolysis leading to precipitation of the proteolysis product at neutral pH suggests that it could contribute to the protein plugging observed in cystic fibrosis (CF). AIMS: To study its behaviour in the serum of CF patients with or without pancreatic insufficiency and to compare it with that of other pancreatic secretory proteins. PATIENTS: 170 patients (93 with CF, 55 controls, and 22 with chronic pancreatitis) were studied. METHODS: Reg protein was measured using a specific enzyme immunoassay and its molecular form in CF sera was characterised by gel filtration. Molecular gene expression was investigated by dot-blot hybridisation. RESULTS: Reg protein was present in all CF sera studied from patients with or without pancreatic insufficiency, and in all cases the level was significantly higher than in controls. Its chromatographic behaviour in CF sera was identical with that of the protein present in normal serum. No correlation was found between the levels of Reg protein and trypsin(ogen) (or lipase) in CF, nor in control sera or normal pancreatic juice. Molecular gene expression of the corresponding proteins investigated in pancreatic tissues showed an absence of correlation between the mRNA levels. CONCLUSIONS: Reg protein may not be a secretory exocrine protein like the digestive enzymes but rather a hormone-like secretory substance with an endocrine or paracrine function.  (+info)

Temperature-jump studies on the interaction of benzeneboronic acid with chymotrypsinogen. (2/124)

The interaction of chymotrypsinogen A with benzeneboronic acid (BBA), a transition state along inhibitor of serine proteases, was investigated by the temperature-jump method using pH indicators. It was found that l/tau is dependent on BBA concentration, in contrast to the case of the alpha-chymotrypsin [EC 3.4.21.1]-BBA system in which l/tau is independent of BBA concentration. By examination of the pH dependences of the kinetic parameters, the acid dissociation behavior of His 57 in chymotrypsinogen, chymotrypsinogen-trigonal BBA complex and chymotrypsinogen-tetrahedral BBA complex was analyzed. The kinetic deuterium isotope effect was also examined and found to occur principally on the acid dissociation constants. The state of the catalytic residues in the zymogen molecule is discussed based on these results.  (+info)

Pancreatic function in CCK-deficient mice: adaptation to dietary protein does not require CCK. (3/124)

A CCK-deficient mouse mutant generated by gene targeting in embryonic stem cells was analyzed to determine the importance of CCK for growth and function of the exocrine pancreas and for pancreatic adaptation to dietary changes. RIAs confirmed the absence of CCK in mutant mice and demonstrated that tissue concentrations of the related peptide gastrin were normal. CCK-deficient mice are viable and fertile and exhibit normal body weight. Pancreas weight and cellular morphology appeared normal, although pancreatic amylase content was elevated in CCK-deficient mice. We found that a high-protein diet increased pancreatic weight, protein, DNA, and chymotrypsinogen content similarly in CCK-deficient and wild-type mice. This result demonstrates that CCK is not required for protein-induced pancreatic hypertrophy and increased proteolytic enzyme content. This is a novel finding, since CCK has been considered the primary mediator of dietary protein-induced changes in the pancreas. Altered somatostatin concentrations in brain and duodenum of CCK-deficient mice suggest that other regulatory pathways are modified to compensate for the CCK deficiency.  (+info)

Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles. (4/124)

We have determined the concentrations of the secretory proteins amylase and chymotrypsinogen and the membrane proteins KDELr and rBet1 in COPII- and COPI-coated pre-Golgi compartments of pancreatic cells by quantitative immunoelectron microscopy. COPII was confined to ER membrane buds and adjacent vesicles. COPI occurred on vesicular tubular clusters (VTCs), Golgi cisternae, the trans-Golgi network, and immature secretory granules. Both secretory proteins exhibited a first, significant concentration step in noncoated segments of VTC tubules and were excluded from COPI-coated tips. By contrast, KDELr and rBet1 showed a first, significant concentration in COPII-coated ER buds and vesicles and were prominently present in COPI-coated tips of VTC tubules. These data suggest an important role of VTCs in soluble cargo concentration by exclusion from COPI-coated domains.  (+info)

Detection of the pancreas-specific gene in the peripheral blood of patients with pancreatic carcinoma. (5/124)

The prognosis of patients with pancreatic carcinoma remains very poor. To improve the therapeutic results, the early detection of this cancer is needed. The present study was performed to detect the pancreas-specific gene, chymotrypsinogen, in the peripheral blood from patients with pancreatic carcinoma by using reverse transcription polymerase chain reaction (RT-PCR) in order to evaluate the clinical significance of this gene. Ten patients with pancreatic carcinoma, two with acute pancreatitis, three with chronic pancreatitis and ten control subjects were examined for the presence of chymotrypsinogen using RT-PCR techniques in the peripheral blood. To confirm that the chymotrypsinogen gene was expressed in a pancreas-specific manner, the expression of chymotrypsinogen in various types of human adult tissue was evaluated by RT-PCR. The specific band of the chymotrypsinogen gene was detected in the pancreas. Serial dilution studies demonstrated the chymotrypsinogen gene to be detected at a concentration of one pancreatic cell per 10(6) peripheral blood cells. Seven out of the ten (70%) patients with pancreatic carcinoma were found to be positive based on the RT-PCR findings. In contrast, no pancreas-specific gene was detected in the peripheral blood of any patients with acute pancreatitis, chronic pancreatitis or the control subjects. Our observations show that the detection of the pancreatic specific gene, chymotrypsinogen, is therefore useful as a genetic diagnostic marker in pancreatic carcinoma.  (+info)

The CCKB/gastrin receptor is coupled to the regulation of enzyme secretion, protein synthesis and p70 S6 kinase activity in acinar cells from ElasCCKB transgenic mice. (6/124)

In order to determine which physiological functions can be regulated by the pancreatic CCKB/gastrin receptor, studies were carried out on pancreatic acini from mice expressing transgenic CCKB/gastrin receptors in the exocrine pancreas (ElasCCKB mice). Acini were stimulated by sulfated gastrin in the presence of SR 27897 (1.8 microM), blocking endogenous CCKA receptors. After 30 min incubation with gastrin, the secretion of chymotrypsinogen and amylase showed superimposable monophasic dose-response curves. Enzyme secretion was detectable and maximal at 100 pM and 1 nM of gastrin, respectively. No increase in chymotrypsinogen and amylase mRNAs was detected for doses of gastrin which specifically occupy the CCKB/gastrin receptor. In contrast, gastrin stimulated total protein synthesis in isolated acini from ElasCCKB mice. [35S]Methionine incorporation into total proteins was increased dose-dependently to a maximum for 30 pM gastrin and inhibited with higher doses (> 300 pM). Gastrin stimulated p70 S6 kinase activity for concentrations ranging from 10 pM to 1 nM. Gastrin-stimulated p70 S6 kinase activity and protein synthesis were blocked by rapamycin and wortmannin. Therefore, in ElasCCKB mice acinar cells, the CCKB/gastrin receptor mediates enzyme release and protein synthesis. However, a more efficient coupling of the CCKB/gastrin receptor to protein synthesis than to enzyme secretion was demonstrated. CCKB/gastrin receptor-stimulated protein synthesis likely results from an enhancement of mRNA translation and involves phosphatidyl inositol 3-kinase and p70 S6 kinase.  (+info)

New structural motifs on the chymotrypsin fold and their potential roles in complement factor B. (7/124)

Factor B and C2 are two central enzymes for complement activation. They are multidomain serine proteases and require cofactor binding for full expression of proteolytic activities. We present a 2.1 A crystal structure of the serine protease domain of factor B. It shows a number of structural motifs novel to the chymotrypsin fold, which by sequence homology are probably present in C2 as well. These motifs distribute characteristically on the protein surface. Six loops surround the active site, four of which shape substrate-binding pockets. Three loops next to the oxyanion hole, which typically mediate zymogen activation, are much shorter or absent. Three insertions including the linker to the preceding domain bulge from the side opposite to the active site. The catalytic triad and non-specific substrate-binding site display active conformations, but the oxyanion hole displays a zymogen-like conformation. The bottom of the S1 pocket has a negative charge at residue 226 instead of the typical 189 position. These unique structural features may play different roles in domain-domain interaction, cofactor binding and substrate binding.  (+info)

Formation of intermediate filament protein aggregates with disparate effects in two transgenic mouse models lacking the neurofilament light subunit. (8/124)

Protein aggregates containing intermediate filaments (IFs) are a hallmark of degenerating spinal motor neurons in amyotrophic lateral sclerosis (ALS). Recently, we reported that a deficiency in neurofilament light subunit (NF-L), a phenomenon associated with ALS, promoted the formation of IF inclusions with ensuing motor neuron death in transgenic mice overproducing peripherin, a type III IF protein detected in axonal inclusions of ALS patients. To further assess the role of NF-L in the formation of abnormal IF inclusions, we generated transgenic mice overexpressing human neurofilament heavy subunits (hNF-H) in a context of targeted disruption of the NF-L gene (hH;L-/- mice). The hH;L-/- mice exhibited motor dysfunction, and they developed nonfilamentous protein aggregates containing NF-H and peripherin proteins in the perikarya of spinal motor neurons. However, the perikaryal protein aggregates in the hH;L-/- mice did not provoke motor neuron death, unlike toxic IF inclusions induced by peripherin overexpression in NF-L null mice (Per;L-/- mice). Our results indicate that different types of IF protein aggregates with distinct properties may occur in a context of NF-L deficiency and that an axonal localization of such aggregates may be an important factor of toxicity.  (+info)

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.

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.

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.

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.

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.

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.

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.

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.

Carboxypeptidase B is a type of enzyme that belongs to the peptidase family. It is also known as carboxypeptidase B1 or CpB. This enzyme plays a crucial role in the digestion of proteins by cleaving specific amino acids from the carboxyl-terminal end of polypeptides.

Carboxypeptidase B preferentially removes basic arginine and lysine residues from protein substrates, making it an essential enzyme in various physiological processes, including blood clotting, hormone processing, and neuropeptide metabolism. It is synthesized as an inactive zymogen, procarboxypeptidase B, which is converted to its active form upon proteolytic activation.

In addition to its physiological functions, carboxypeptidase B has applications in research and industry, such as protein sequencing, peptide synthesis, and food processing.

Ceruletide is a synthetic analog of the natural hormone cholecystokinin (CCK). It is a decapeptide with the following sequence: cyclo(D-Asp-Tic-Phe-Ser-Leu-Hand-Ala-Lys-Thr-Nle-NH2).

Ceruletide has several pharmacological actions, including stimulation of the release of digestive enzymes from the pancreas, contraction of the gallbladder and sphincter of Oddi, and inhibition of gastric acid secretion. It is used in clinical medicine for diagnostic purposes to test the motor function of the biliary tract and to diagnose gastrointestinal motility disorders.

Ceruletide has also been investigated as a potential treatment for certain conditions such as pancreatitis, gallstones, and intestinal obstruction, but its use is limited due to its side effects, which include nausea, vomiting, abdominal cramps, and diarrhea.

Cholecystokinin (CCK) is a hormone that is produced in the duodenum (the first part of the small intestine) and in the brain. It is released into the bloodstream in response to food, particularly fatty foods, and plays several roles in the digestive process.

In the digestive system, CCK stimulates the contraction of the gallbladder, which releases bile into the small intestine to help digest fats. It also inhibits the release of acid from the stomach and slows down the movement of food through the intestines.

In the brain, CCK acts as a neurotransmitter and has been shown to have effects on appetite regulation, mood, and memory. It may play a role in the feeling of fullness or satiety after eating, and may also be involved in anxiety and panic disorders.

CCK is sometimes referred to as "gallbladder-stimulating hormone" or "pancreozymin," although these terms are less commonly used than "cholecystokinin."

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.

Lipase is an enzyme that is produced by the pancreas and found in the digestive system of most organisms. Its primary function is to catalyze the hydrolysis of fats (triglycerides) into smaller molecules, such as fatty acids and glycerol, which can then be absorbed by the intestines and utilized for energy or stored for later use.

In medical terms, lipase levels in the blood are often measured to diagnose or monitor conditions that affect the pancreas, such as pancreatitis (inflammation of the pancreas), pancreatic cancer, or cystic fibrosis. Elevated lipase levels may indicate damage to the pancreas and its ability to produce digestive enzymes.

Muramidase, also known as lysozyme, is an enzyme that hydrolyzes the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, a polymer found in bacterial cell walls. This enzymatic activity plays a crucial role in the innate immune system by contributing to the destruction of invading bacteria. Muramidase is widely distributed in various tissues and bodily fluids, such as tears, saliva, and milk, and is also found in several types of white blood cells, including neutrophils and monocytes.

Enteropeptidase, also known as enterokinase, is an enzyme that is produced by the intestinal brush border cells. Its primary function is to activate other digestive enzymes, most notably trypsinogen, which is a precursor to the digestive enzyme trypsin.

Trypsinogen is inactive until it is cleaved by enteropeptidase, which removes a small peptide from the N-terminus of the molecule, activating it and allowing it to participate in protein digestion. Enteropeptidase also plays a role in activating other zymogens, such as chymotrypsinogen and procarboxypeptidases, which are involved in the breakdown of proteins and peptides in the small intestine.

Deficiency or absence of enteropeptidase can lead to malabsorption and impaired digestion, as the activation of other digestive enzymes is hindered.

Celiac disease is a genetic autoimmune disorder in which the consumption of gluten, a protein found in wheat, barley, and rye, leads to damage in the small intestine. In people with celiac disease, their immune system reacts to gluten by attacking the lining of the small intestine, leading to inflammation and destruction of the villi - finger-like projections that help absorb nutrients from food.

This damage can result in various symptoms such as diarrhea, bloating, fatigue, anemia, and malnutrition. Over time, if left untreated, celiac disease can lead to serious health complications, including osteoporosis, infertility, neurological disorders, and even certain types of cancer.

The only treatment for celiac disease is a strict gluten-free diet, which involves avoiding all foods, beverages, and products that contain gluten. With proper management, individuals with celiac disease can lead healthy lives and prevent further intestinal damage and related health complications.

Glycodeoxycholic acid (GDCA) is not a widely recognized or established medical term. However, it appears to be a chemical compound that can be formed as a result of the metabolic process in the body. It is a glycine-conjugated bile acid, which means that it is a combination of the bile acid deoxycholic acid and the amino acid glycine.

Bile acids are produced by the liver to help with the digestion and absorption of fats in the small intestine. They are conjugated, or combined, with amino acids like glycine or taurine before being released into the bile. These conjugated bile acids help to keep the bile acid salts in their soluble form and prevent them from being reabsorbed back into the bloodstream.

Glycodeoxycholic acid may be involved in various physiological processes, but there is limited research on its specific functions or medical significance. If you have any concerns about this compound or its potential impact on your health, it would be best to consult with a healthcare professional for more information.

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.

The duodenum is the first part of the small intestine, immediately following the stomach. It is a C-shaped structure that is about 10-12 inches long and is responsible for continuing the digestion process that begins in the stomach. The duodenum receives partially digested food from the stomach through the pyloric valve and mixes it with digestive enzymes and bile produced by the pancreas and liver, respectively. These enzymes help break down proteins, fats, and carbohydrates into smaller molecules, allowing for efficient absorption in the remaining sections of the small intestine.

Glycylglycine is not a medical condition or term, but rather it is a chemical compound. It is a dipeptide, which means it is composed of two amino acids linked together. Specifically, glycylglycine consists of two glycine molecules joined by an amide bond (also known as a peptide bond) between the carboxyl group of one glycine and the amino group of the other glycine.

Glycylglycine is often used in laboratory research as a buffer, a substance that helps maintain a stable pH level in a solution. It has a relatively simple structure and is not naturally found in significant amounts in living organisms.

... must be inactive until it gets to the digestive tract. This prevents damage to the pancreas or any other ... Chymotrypsinogen is a single polypeptide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of ... Chymotrypsinogen is an inactive precursor (zymogen) of chymotrypsin, a digestive enzyme which breaks proteins down into smaller ... The Activation of Chymotrypsinogen". Biochemistry. 6 (2): 567-572. doi:10.1021/bi00854a026. ISSN 0006-2960. PMID 6047640. v t e ...
... is a protein that in humans is encoded by the CTRB2 gene. ENSG00000284810 GRCh38: Ensembl release 89: ... "Entrez Gene: Chymotrypsinogen B2". Retrieved 2018-04-17. v t e (Articles with short description, Short description matches ...
Its precursor is chymotrypsinogen. Trypsin activates chymotrypsinogen by cleaving peptidic bonds in positions Arg15 - Ile16 and ... Wilcox PE (1970). "[5] Chymotrypsinogens-chymotrypsins". Chymotrypsinogens - chymotrypsins. Methods in Enzymology. Vol. 19. pp ... Trypsin PA clan of proteases PDB: 1CHG​; Freer ST, Kraut J, Robertus JD, Wright HT, Xuong NH (April 1970). "Chymotrypsinogen: ...
Chymotrypsinogen B2 is a protein that in humans is encoded by the CTRB2 gene. ENSG00000284810 GRCh38: Ensembl release 89: ... "Entrez Gene: Chymotrypsinogen B2". Retrieved 2018-04-17. v t e (Articles with short description, Short description matches ...
Wilcox PE (1970). "Chymotrypsinogens - chymotrypsins". Methods Enzymol. Methods in Enzymology. 19: 64-108. doi:10.1016/0076- ... This enzyme is formed from pig chymotrypsinogen C and from cattle subunit II of procarboxypeptidase A. Elastase 4 Peanasky RJ, ... "Mode of activation of N-terminal sequence of subunit II in bovine procarboxypeptidase A and of porcine chymotrypsinogen C". ...
Walsh KA, Neurath H (1964). "Trypsinogen and Chymotrypsinogen as Homologous Proteins". Proc. Natl. Acad. Sci. U.S.A. 52 (4): ...
Chymotrypsinogen can also be activated by trypsin. Carboxypeptidase, which is a protease that takes off the terminal amino acid ... Chymotrypsinogen, which is an inactive (zymogenic) protease that, once activated by duodenal enterokinase, turns into ...
Fersht AR, Sperling J (February 1973). "The charge relay system in chymotrypsin and chymotrypsinogen". J. Mol. Biol. 74 (2): ...
In particular, he has determined the complete amino acid sequence of chymotrypsinogen, a protein of 253 residues, and has ... Hartley, B. S. (1964). "Amino-Acid Sequence of Bovine Chymotrypsinogen-A". Nature. 201 (4926): 1284-1287. Bibcode:1964Natur. ... The disulphide bridges of bovine chymotrypsinogen A". Biochemical Journal. 101 (1): 214-228. doi:10.1042/bj1010214. PMC 1270086 ...
Uptake of Glycine-N15 by the Trypsinogen and Chymotrypsinogen of Mouse Pancreas" (PDF). Journal of General Physiology. 39 (2): ...
The major proteases, the pancreatic enzymes which work on proteins, are trypsinogen and chymotrypsinogen. Elastase is also ...
Freer ST, Kraut J, Robertus JD, Tonle H, Wright HT (1970). "Chymotrypsinogen: 2.5-Å crystal structure, comparison with α- ... The early crystal structures included chymotrypsin (PDB file 2CHA), chymotrypsinogen (PDB file 1CHG), trypsin (PDB file 1PTN), ...
2008). "Association of rare chymotrypsinogen C (CTRC) gene variations in patients with idiopathic chronic pancreatitis". Hum. ...
It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. It is cleaved ...
Determination of the thermodynamic stability of chymotrypsinogen A and ribonuclease A in glycerol". J. Phys. Chem. 100 (17): ...
The free trypsin then cleaves the rest of the trypsinogen, as well as chymotrypsinogen to its active form chymotrypsin. Enzymes ... in the exocrine cellular compartment and have functions related to digestion or food uptake such as digestive chymotrypsinogen ...
"Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic ...
"Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic ...
... specificity and genomic structures of human neutrophil elastase and cathepsin G reveal a new branch of the chymotrypsinogen ...
... such as the serine protease precursors trypsinogen and chymotrypsinogen, and the aspartic protease precursor pepsinogen. The ...
The function of this is to protect the animal from any accidental activation of trypsinogen and/or chymotrypsinogen Trypsin ... It is formed in the pancreas and activated to trypsin with enteropeptidase Chymotrypsinogen is the inactive form of ...
Trypsin then cleaves and activates other pancreatic serine protease zymogens (chymotrypsinogen and proelastases), ... such as chymotrypsinogen, proelastase, procarboxypeptidase and prolipase in the lumen of the gut. As the pro-region of ...
Chymotrypsinogen, is single polypeptide chain of 245 amino acids residues, is converted to alpha-chymotrypsin, which has three ... Examples of zymogens: Trypsinogen Chymotrypsinogen Pepsinogen Most proteins in the coagulation system (examples, prothrombin, ... In the duodenum, the pancreatic zymogens, trypsinogen, chymotrypsinogen, proelastase and procarboxypeptidase are converted into ... polypeptide chains linked by two of the five disulfide bond present in the primary structure of chymotrypsinogen. ...
Chymotrypsin, a digestive protease, is produced in inactive form as chymotrypsinogen in the pancreas and transported in this ...
... chymotrypsinogen, elastase, carboxypeptidase, pancreatic lipase, nucleases and amylase. The pancreas is located in the visceral ...
Chymotrypsinogen must be inactive until it gets to the digestive tract. This prevents damage to the pancreas or any other ... Chymotrypsinogen is a single polypeptide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of ... Chymotrypsinogen is an inactive precursor (zymogen) of chymotrypsin, a digestive enzyme which breaks proteins down into smaller ... The Activation of Chymotrypsinogen". Biochemistry. 6 (2): 567-572. doi:10.1021/bi00854a026. ISSN 0006-2960. PMID 6047640. v t e ...
chymotrypsinogen, buboes, kymographic, repechage, dicotyledonous, chlorophyllous, zalcitabine, scintigraphy, ciguatera.. ORAL ...
In turn, trypsin activates the other pancreatic proteolytic zymogens (chymotrypsinogen, procarboxypeptidase, proelastase) to ...
Die Aktivierung von Chymotrypsinogen zu Chymotrypsin. F. Šorm, B. Keil and I. Rychlík ...
Affinity DataIC50: 4.00E+4nMAssay Description:Inhibitory activity against chymotrypsinogenMore data for this Ligand-Target Pair ...
Chymotrypsinogen synthesis in the exocrine cell of the guinea pig pancreas was studied under the following conditions: Animals ... A Cytochemical Study on the Pancreas of the Guinea Pig : V. In vivo Incorporation of Leucine-1-C14 into the Chymotrypsinogen of ... Chymotrypsinogen synthesis in the exocrine cell of the guinea pig pancreas was studied under the following conditions: Animals ... The chymotrypsinogen isolated from the attached ribonucleoprotein particles of the microsomal fraction had the highest specific ...
... chymotrypsinogen A (25,000) and RNase A (13,700) (page 1602, Figure 1 description, two lines from the bottom). From the elution ...
THREE-DIMENSIONAL STRUCTURE OF THE COMPLEXES BETWEEN BOVINE CHYMOTRYPSINOGEN*A AND TWO RECOMBINANT VARIANTS OF HUMAN PANCREATIC ... THREE-DIMENSIONAL STRUCTURE OF THE COMPLEXES BETWEEN BOVINE CHYMOTRYPSINOGEN*A AND TWO RECOMBINANT VARIANTS OF HUMAN PANCREATIC ...
Vendrell, J., Catasús, L., Oppezzo, O., Ventura, S., Villegas, V. & Avilés, F. X., 1 Jan 1993, Innovations in proteases and their inhibitors.. Avilés, F. X. (ed.). 1 ed. Berlín (DE), p. 279-297 18 p. (Innovations in proteases and their inhibitors).. Research output: Chapter in Book › Chapter › Research › peer-review ...
It originated as the Phoenician symbol nun, adopted by the Greeks as n… Chymotrypsinogen , chymotrypsinogen (ky-moh-trip-sin-ŏ- ...
α -Chymotrypsinogen A 25,700. Uricase. 128,000. α -Chymotrypsin 25,200. Choline Oxidase. 95,000 Trypsinogen 24,000. ...
The conversion of chymotrypsinogen to chymotrypsin is catalyzed by trypsin, which in turn arises from trypsinogen as a result ... When chymotrypsinogen is secreted into the small intestine, trypsin present in the digestive system cleaves the peptide bond ... Chymotrypsinogen lacks this bond; therefore, it does not have the active conformation and cannot bind substrate.. ... Chymotrypsinogen consists of a single polypeptide chain 245 residues long, with five disulfide (-S-S-) bonds. ...
3. The activation of chymotrypsinogen. (1967). (42). *. Developmentally regulated expression of the cold-inducible RNA-binding ...
Chymotrypsinogen-like protein 3 n=9 Tax=Obtectomera RepID=A5CG73_MANSE. NCBI RefSeq. NP_001166253.1. 4e-28. 34.43%. serine ...
Pancreatic juice is secreted by the pancreas, which contains a vriety of enzymes, including trypsinogen, chymotrypsinogen, ...
The Common Chymotrypsinogen C (CTRC) Variant G60G (C.180T) Increases Risk of Chronic Pancreatitis But Not Recurrent Acute ... Chymotrypsinogen C (CTRC) protects the pancreas by degrading prematurely activated trypsinogen. Rare mutations are associated ...
... chymotrypsinogen and procarboxypeptidase, and the enzyme pancreatic lipase. Pancreatic juice aids in the digestion of proteins ...
Chymotrypsinogen: Chymotrypsinogen when converted to active form chymotrypsin it converts polypeptides to dipeptides. ...
A, Chymotrypsinogen A, Coenzyme A, Colipase A, Concanavalin A, Cyclophilin A, Exfoliatin Toxin A, Fibrinopeptide A, ...
Chymotrypsinogen -- The inactive proenzyme secreted by the pancreas that is subsequently converted to chymotrypsin. ...
Chymotrypsinogen is produced by. काइमोट्रिप्सिनोजन किसके द्वारा उत्पन्न किया जाता है: (1) (3) (2) (4) ...
... chymotrypsinogen is activated by trypsin to form chymotrypsin Note: pepsin, trypsin and chymotrypsin are all endopeptidases • ...
It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. ...
PRP is a solution for intravenous administration of a combination of two pancreatic proenzymes trypsinogen and chymotrypsinogen ...
PRP is a mixture of two proenzymes, trypsinogen and chymotrypsinogen from bovine pancreas administered by intravenous injection ... trypsinogen and chymotrypsinogen. Dr Kenyon concluded that no severe or serious adverse events related to the rectal ...
Ultra-rapid glutathionylation of chymotrypsinogen in its molten globule-like conformation: A comparison to archaeal proteins ( ...
Natural single-nucleotide deletion in chymotrypsinogen C gene increases severity of secretagogue-induced pancreatitis in C57BL/ ...
  • Their inactive precursor molecules, trypsinogen and chymotrypsinogen, respectively, are formed in the pancreas, where they would do damage if they were in an active form. (brainkart.com)
  • PRP is a solution for intravenous administration of a combination of two pancreatic proenzymes trypsinogen and chymotrypsinogen. (propanc.com)
  • Clinical experience was obtained via a compassionate use study in 46 late-stage cancer patients using a suppository formulation of two proenzymes, trypsinogen and chymotrypsinogen. (dailytimesleader.com)
  • [2] The enzymes include proteases (trypsinogen and chymotrypsinogen), hydrolytic enzymes that cleave lipids (the lipases phospholipase A2 and lysophospholipase, and cholesterol esterase), and amylase to digest starches. (iiab.me)
  • Following the isolation of trypsinogen and chymotrypsinogen as specific proteins, DNase 1 was isolated in crystalline form from bovine pancreas and shown to be a heat sensitive protein that could cleave thymus DNA (16). (pancreapedia.org)
  • Chymotrypsinogen is an inactive precursor (zymogen) of chymotrypsin, a digestive enzyme which breaks proteins down into smaller peptides. (wikipedia.org)
  • TNS forms covalent bonds with chymotrypsinogen and as the bonds break to form chymotrypsin in the presence of trypsin the fluorescence increases. (wikipedia.org)
  • Trypsin activates chymotrypsinogen and procarboxypeptidase into chymotrypsin and carboxypeptidase respectively.typsin also actson proteoses and peptones and changes them to peptides. (preservearticles.com)
  • The conversion of chymotrypsinogen to chymotrypsin is catalyzed by trypsin, which in turn arises from trypsinogen as a result of a cleavage reaction catalyzed by the enzyme enteropeptidase. (brainkart.com)
  • Chymotrypsinogen -- The inactive proenzyme secreted by the pancreas that is subsequently converted to chymotrypsin. (nih.gov)
  • Some of the enzymes that are produced by the pancreas are trypsinogen, chymotrypsinogen, carboxypeptidase, and lipase. (clinicaleducation.org)
  • It not just has the features of digestive enzymes, but also can restrict the decomposition of other forerunners of various Enzymes such as chymotrypsinogen, carboxypeptidase, as well as phospholipase, and work as an activation feature. (zhishangchemical.com)
  • Results Initial discovery GWAS detected SNPs within or near genes encoding the ABO blood group specifying transferases A/B ( ABO ), Fucosyltransferase-2 ( FUT2 ), and Chymotrypsinogen-B2 ( CTRB2 ), to be significantly associated with lipase activity levels in asymptomatic subjects. (bmj.com)
  • Pancreatic juice contains the enzymes trypsinogen, chymotrypsinogen, amylase and lipase. (peterdobias.com)
  • It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. (examveda.com)
  • Chymotrypsinogen synthesis in the exocrine cell of the guinea pig pancreas was studied under the following conditions: Animals fed after a fast of ∼48 hours received ∼1 hour after feeding an intravenous injection of DL -leucine-1-C 14 . (rupress.org)
  • Chymotrypsinogen C (CTRC) protects the pancreas by degrading prematurely activated trypsinogen. (bvsalud.org)
  • Chymotrypsinogen is a single polypeptide chain consisting of 245 amino acid residues. (wikipedia.org)
  • Chymotrypsinogen consists of a single polypeptide chain 245 residues long, with five disulfide (-S-S-) bonds. (brainkart.com)
  • Chymotrypsinogen must be inactive until it gets to the digestive tract. (wikipedia.org)
  • Calorimetric studies of the activation of chymotrypsinogen A". Biochemistry. (wikipedia.org)
  • From each cell fraction, the chymotrypsinogen was isolated by acid extraction and purified by (NH 4 ) 2 SO 4 fractionation, isoelectric precipitation, and chromatography. (rupress.org)
  • The chymotrypsinogen isolated from the attached ribonucleoprotein particles of the microsomal fraction had the highest specific radioactivity at the early time points (1 to 3 minutes). (rupress.org)
  • Trypsin cleaves the peptide bond in chymotrypsinogen between arginine-15 and isoleucine-16. (wikipedia.org)
  • When chymotrypsinogen is secreted into the small intestine, trypsin present in the digestive system cleaves the peptide bond between arginine 15 and isoleucine 16, counting from the N-terminal end of the chymotrypsinogen sequence (Figure 7.10). (brainkart.com)
  • Because of the minuteness of the quantities involved, chymotrypsinogen amounts were calculated from enzymatic activity figures, and a carrier method was used to precipitate and count the enzyme. (rupress.org)
  • Later, additional genes coding for proteins that affect trypsin activation, such as the chymotrypsinogen C gene and calcium sensing receptor gene, were also found to contribute to pancreatitis susceptibility. (nih.gov)
  • These include alterations in genes coding for trypsinogens, the most abundant digestive enzymes (PRSS1 and PRSS2), the trypsin inhibitor (SPINK1) and the trypsin-degrading enzyme, chymotrypsinogen C (CTRC). (nih.gov)
  • The Common Chymotrypsinogen C (CTRC) Variant G60G (C.180T) Increases Risk of Chronic Pancreatitis But Not Recurrent Acute Pancreatitis in a North American Population. (cdc.gov)
  • This gene is located adjacent to a related chymotrypsinogen gene. (nih.gov)
  • lysozyme, ribonuclease A, cytochrome C, α-chymotrypsinogen, α-lactalbumin, ovalbumin, transferrin, and myoglobin were baseline separated within 25 min by 25 mM sodium phosphate buffers (pH 7.0) containing 100 µg/mL QC. (go.jp)
  • Calorimetric studies of the activation of chymotrypsinogen A". Biochemistry. (wikipedia.org)