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.
The largest of the three pairs of SALIVARY GLANDS. They lie on the sides of the FACE immediately below and in front of the EAR.
Enzymes that catalyze the endohydrolysis of 1,4-alpha-glycosidic linkages in STARCH; GLYCOGEN; and related POLYSACCHARIDES and OLIGOSACCHARIDES containing 3 or more 1,4-alpha-linked D-glucose units.
INFLAMMATION of the PANCREAS. Pancreatitis is classified as acute unless there are computed tomographic or endoscopic retrograde cholangiopancreatographic findings of CHRONIC PANCREATITIS (International Symposium on Acute Pancreatitis, Atlanta, 1992). The two most common forms of acute pancreatitis are ALCOHOLIC PANCREATITIS and gallstone pancreatitis.
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.
The clear, viscous fluid secreted by the SALIVARY GLANDS and mucous glands of the mouth. It contains MUCINS, water, organic salts, and ptylin.
An enzyme that hydrolyzes 1,6-alpha-glucosidic branch linkages in glycogen, amylopectin, and their beta-limit dextrins. It is distinguished from pullulanase (EC 3.2.1.41) by its inability to attack pullulan and by the feeble action of alpha-limit dextrins. It is distinguished from amylopectin 6-glucanohydrolase (EC 3.2.1.69) by its action on glycogen. With EC 3.2.1.69, it produces the activity called "debranching enzyme". EC 3.2.1.68.
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.
The fluid containing digestive enzymes secreted by the pancreas in response to food in the duodenum.
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.
Any of a group of polysaccharides of the general formula (C6-H10-O5)n, composed of a long-chain polymer of glucose in the form of amylose and amylopectin. It is the chief storage form of energy reserve (carbohydrates) in plants.
An octapeptide hormone present in the intestine and brain. When secreted from the gastric mucosa, it stimulates the release of bile from the gallbladder and digestive enzymes from the pancreas.
A subclass of alpha-amylase ISOENZYMES that are secreted into SALIVA.
The inactive proenzyme of trypsin secreted by the pancreas, activated in the duodenum via cleavage by enteropeptidase. (Stedman, 25th ed)
Chymotrypsinogen is a precursor protein that is converted into the digestive enzyme chymotrypsin in the pancreas and small intestine.
A condition with abnormally elevated level of AMYLASES in the serum. Hyperamylasemia due to PANCREATITIS or other causes may be differentiated by identifying the amylase isoenzymes.
The major component (about 80%) of the PANCREAS composed of acinar functional units of tubular and spherical cells. The acinar cells synthesize and secrete several digestive enzymes such as TRYPSINOGEN; LIPASE; AMYLASE; and RIBONUCLEASE. Secretion from the exocrine pancreas drains into the pancreatic ductal system and empties into the DUODENUM.
Bethanechol compounds are drugs that stimulate the muscarinic receptors in the body, particularly in the smooth muscles of the bladder and the pupils of the eye, to increase urine flow and dilate the pupils, respectively.
Proteins and peptides found in SALIVA and the SALIVARY GLANDS. Some salivary proteins such as ALPHA-AMYLASES are enzymes, but their composition varies in different individuals.
The amount of a substance secreted by cells or by a specific organ or organism over a given period of time; usually applies to those substances which are formed by glandular tissues and are released by them into biological fluids, e.g., secretory rate of corticosteroids by the adrenal cortex, secretory rate of gastric acid by the gastric mucosa.
A peptide hormone of about 27 amino acids from the duodenal mucosa that activates pancreatic secretion and lowers the blood sugar level. (USAN and the USP Dictionary of Drug Names, 1994, p597)
A dextrodisaccharide from malt and starch. It is used as a sweetening agent and fermentable intermediate in brewing. (Grant & Hackh's Chemical Dictionary, 5th ed)
Disease having a short and relatively severe course.
Pathological processes of the PANCREAS.
Analyses for a specific enzyme activity, or of the level of a specific enzyme that is used to assess health and disease risk, for early detection of disease or disease prediction, diagnosis, and change in disease status.
A subclass of alpha-amylase ISOENZYMES that are secreted into PANCREATIC JUICE.
Oligosaccharides containing three monosaccharide units linked by glycosidic bonds.
A slowly hydrolyzed CHOLINERGIC AGONIST that acts at both MUSCARINIC RECEPTORS and NICOTINIC RECEPTORS.
Liver disease in which the normal microcirculation, the gross vascular anatomy, and the hepatic architecture have been variably destroyed and altered with fibrous septa surrounding regenerated or regenerating parenchymal nodules.
FIBROSIS of the hepatic parenchyma due to obstruction of BILE flow (CHOLESTASIS) in the intrahepatic or extrahepatic bile ducts (BILE DUCTS, INTRAHEPATIC; BILE DUCTS, EXTRAHEPATIC). Primary biliary cirrhosis involves the destruction of small intra-hepatic bile ducts and bile secretion. Secondary biliary cirrhosis is produced by prolonged obstruction of large intrahepatic or extrahepatic bile ducts from a variety of causes.
An activity in which the body advances at a slow to moderate pace by moving the feet in a coordinated fashion. This includes recreational walking, walking for fitness, and competitive race-walking.
FIBROSIS of the hepatic parenchyma due to chronic excess ALCOHOL DRINKING.
Physical activity which is usually regular and done with the intention of improving or maintaining PHYSICAL FITNESS or HEALTH. Contrast with PHYSICAL EXERTION which is concerned largely with the physiologic and metabolic response to energy expenditure.
Experimentally induced chronic injuries to the parenchymal cells in the liver to achieve a model for LIVER CIRRHOSIS.
A lack of HYDROCHLORIC ACID in GASTRIC JUICE despite stimulation of gastric secretion.

The structure of a glycopeptide (GP-II) isolated from Rhizopus saccharogenic amylase. (1/1858)

Mild alkaline treatment of glycopeptide (GP-II) resulted in the loss of 1 mole of serine and 5 moles of threonine per mole of GP-II, suggesting the presence of O-glycosyl bonds between 1 serine and 5 threonine residues and carbohydrate chains. Treatment of GP-II with alkaline borohydride released only disaccharide. Methylation studies of the carbohydrate moiety gave 2,3,4,6-tetra-O-methyl and 2,4,6-tri-O-methyl derivatives of mannose in a ratio of approximately 1:1. In addition, one step of Smith degradation resulted in the loss of about 6 residues of mannose per mole of GP-II. Moreover, alpha-mannosidase [EC 3.2.1.24] liberated about 6 residles of mannose per mole of GP-II. On the basis of these data, the structure of the carbohydrate moiety of GP-II was confirmed to be 3-O-alpha-mannosylmannose. The amino- and carboxyl-terminal amino acids of GP-II were determined to be threonine and serine, respectively. On reductive cleavage of N-proline bonds with metallic sodium in liquid ammonia, 2 moles of alanine per mole of GP-II were lost. From the compositions of three fragments isolated from the reductive cleavage products, the amino acid sequence of the peptide portion of GP-II was determined. Based on these data, a probable structure was proposed for GP-II.  (+info)

Purification of gibberellic acid-induced lysosomes from wheat aleurone cells. (2/1858)

Using isopycnic density gradient centrifugation, lysosomes were concentrated in a single region of a sucrose-Ficoll gradient (p = 1-10 g cm-3), well separated from most other cell organelles. Gibberellic acid-induced lysosomes were found to be rich in alpha-amylase and protease but not ribonuclease. The lysosomal band also contained a majority of the NADH2-cytochrome c reductase, a marker enzyme for endoplasmic reticulum, found in the gradient. Examination of electron micrographs revealed that a purified band of lyosomes contained at least 3 vesicle types, ranging in size from 0-1 to 0-5 mum. The significance of these findings to proposed mechanisms of action of gibberellic acid is discussed.  (+info)

Detection of viruses and body fluids which may contain viruses in the domestic environment. (3/1858)

The domestic environment was investigated for the presence of viruses and body fluids that may contain viruses. A range of surfaces in 39 homes (17 visited on 2 occasions) were sampled by swabbing and analysed using cell culture, reverse transcription polymerase chain reaction for enteroviral RNA, haemoglobin as a marker for blood, amylase as an indicator of urine, saliva and sweat, and protein as an indicator of general hygiene. Haemoglobin was found on 1.9% of surfaces sampled and of the positive samples 30% were from articles frequently handled. Amylase (> 5 U/l) was found in 29.3% of samples tested. Protein was found in 97.8% of samples tested. Enteroviral RNA, indicating the presence of virus, was detected in 3 out of 448 samples tested; they were from a tap handle, telephone handpiece and a toilet bowl. No viruses were isolated in cell culture, however significant problems were encountered with bacterial and fungal contamination. This work demonstrates that only testing environmental samples for bacteria and ATP may not give a total view of the microbiological problem in the home. A range of test methods is useful to gain a broad view of the problems of hygiene in the home and to allow comparative studies of specific areas such as the kitchen and bathroom.  (+info)

Underestimation of acute pancreatitis: patients with only a small increase in amylase/lipase levels can also have or develop severe acute pancreatitis. (4/1858)

BACKGROUND: In most treatment studies on acute pancreatitis, pancreatologists base their diagnosis on amylase/lipase levels more than three times above the upper limit of normal (>3n) and thus exclude patients with smaller enzyme level increases. The recommendations derived from the results of treatment studies do not take into account such patients. Non-pancreatologists frequently believe that only patients with high enzyme levels have a serious prognosis. AIMS: To question the assumption that high enzyme levels indicate severe, and conversely low enzyme levels indicate mild, acute pancreatitis. PATIENTS/METHODS: This retrospective study includes 284 consecutive patients with a first attack of acute pancreatitis. The cause was biliary in 114 (40%) patients, alcoholism in 83 (29%), other in 21 (7%), and unknown in 66 (23%). Patients were divided into two groups according to their serum enzyme levels (amylase: 3n, n = 196; lipase: 3n, n = 233). Renal impairment, indication for dialysis and artificial ventilation, development of pseudocysts, necessity for surgery, and mortality were taken as parameters of severity. RESULTS: The incidence of severity was the same for both the 3n groups. CONCLUSIONS: The severity of acute pancreatitis is independent of the elevation in serum amylase/lipase level (3n) on admission. Patients with only a slight increase can also have or develop severe acute pancreatitis. Patients with +info)

Genetic regulation of tissue-specific expression of amylase structural genes in Drosophila melanogaster. (5/1858)

Laboratory strains of Drosophila melanogaster were screened for spatial variations in adult midgut alpha-amylase (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1) expression. No strain-specific differences were found anteriorly, but three patterns of activity were discerned in the posterior midgut: A, activity throughout most of the region; B, activity in the anterior part of the region; and C, little or no activity. Alleles of a control gene, map, are responsible for this tissue-specific regulation of activity; e.g., mapA homozygotes produce the A pattern and mapC homozygotes the C pattern. The map locus was placed at 2--80 +/- on the genetic map of chromosome 2R, about two crossover units distal to the Amy structural gene region for alpha-amylase. Electrophoretic studies showed that mapA is trans acting in mapA/mapC flies, allowing expression of amylase isozymes coded for by genes on the opposite chromosome. The map gene behaves as a temporal gene that is clearly separable from the tightly linked, duplicated Amy structural genes.  (+info)

Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain. (6/1858)

A maltogenic amylase gene was cloned in Escherichia coli from a gram-negative thermophilic bacterium, Thermus strain IM6501. The gene encoded an enzyme (ThMA) with a molecular mass of 68 kDa which was expressed by the expression vector p6xHis119. The optimal temperature of ThMA was 60 degrees C, which was higher than those of other maltogenic amylases reported so far. Thermal inactivation kinetic analysis of ThMA indicated that it was stabilized in the presence of 10 mM EDTA. ThMA harbored both hydrolysis and transglycosylation activities. It hydrolyzed beta-cyclodextrin and starch mainly to maltose and pullulan to panose. ThMA not only hydrolyzed acarbose, an amylase inhibitor, to glucose and pseudotrisaccharide (PTS) but also transferred PTS to 17 sugar acceptors, including glucose, fructose, maltose, cellobiose, etc. Structural analysis of acarbose transfer products by using methylation, thin-layer chromatography, high-performance ion chromatography, and nuclear magnetic resonance indicated that PTS was transferred primarily to the C-6 of the acceptors and at lower degrees to the C-3 and/or C-4. The transglycosylation of sugar to methyl-alpha-D-glucopyranoside by forming an alpha-(1,3)-glycosidic linkage was demonstrated for the first time by using acarbose and ThMA. Kinetic analysis of the acarbose transfer products showed that the C-4 transfer product formed most rapidly but readily hydrolyzed, while the C-6 transfer product was stable and accumulated in the reaction mixture as the main product.  (+info)

Ultrastructural analysis of some functional aspects of Xenopus laevis pancreas during development and metamorphosis. (7/1858)

Morphological studies using both light and electron microscope were carried out with the aim of characterizing cells present in the larval and adult pancreas of Xenopus laevis. The following cell types have been seen: (1) exocrine cells, with a very well developed r.e.r. (rough endoplasmic reticulum), well defined Golgi complexes and numerous large secretory granules (A cells); (2) cells without either r.e.r. or secretory granules but with a large number of well developed mitochondria (B cells); (3) endocrine cells often clustered in the typical islets and with small membrane-coated granules showing a very dense central core surrounded by a light halo (C cells). During development, the aspect is seen to change from an unorganized tissue in which the acinar structures are still not clearly visible (stage 42), to a more organized form in which the exocrine cells (A cells) are seen to be arranged around the lumen of the acinus together with some B cells. At the stages 54-56, an increasing number of acini surrounded both by A and B cells was observed. At about stage 61, large quantities of necrotic cells were seen and it became more difficult to individualize the acinar organization found in the preceding stages. Finally, there are no necrotic cells in the adult but only A, B cells which are organized in well developed acinar structures and C cells. The investigation also included a study of some pancreatic enzymes (lipase and amylase) synthesized during larval life. Lipase activity shows a peak at stage 54-56 in which the most well organized tissue of the entire larval life was observed. The activity then decreases, reaching a minimum at stage 66, after which it rapidly rises. Maximum amylase activity occurs at stage 51 after which there is a decrease, to a minimum at stage 66. The activity then remains at constant level.  (+info)

A monoclonal anti-interleukin 8 antibody (WS-4) inhibits cytokine response and acute lung injury in experimental severe acute necrotising pancreatitis in rabbits. (8/1858)

BACKGROUND: Interleukin 8 (IL-8) has recently been proposed to have an important role in mediating the development of the systemic sequelae associated with severe acute pancreatitis. AIMS: To define the role of IL-8 in acute pancreatitis by neutralising its effects with a monoclonal anti-IL-8 antibody (WS-4), in a rabbit model of severe acute pancreatitis. METHODS: Acute pancreatitis was induced by retrograde injection of 5% chenodeoxycholic acid into the pancreatic duct and duct ligation. Twenty rabbits were divided equally into two groups: acute pancreatitis controls received physiological saline and the treated group received WS-4, 30 minutes before induction of acute pancreatitis. RESULTS: Pretreatment of animals with WS-4 resulted in significant down regulation of serum IL-8 and tumour necrosis factor alpha (TNF-alpha) from three to six hours after induction of acute pancreatitis (p = 0.011 and 0.047 for IL-8 and 0.033 and 0.022 for TNF-alpha, respectively). In addition, a significant reduction in the CD11b and CD18 positive cells and the amount of interstitial neutrophil infiltration in the lungs from WS-4 treated animals was seen. In contrast, WS-4 did not alter the amount of pancreatic necrosis and the serum concentrations of amylase, lipase, calcium, and glucose. CONCLUSION: WS-4 cannot change the amount of pancreatic necrosis induced by injection of 5% bile acid, but does reduce the acute lung injury, presumably through inhibition of circulating IL-8 and TNF-alpha, and CD11b/CD18 in lung tissue. Therefore, a role of IL-8 in the progression of acute pancreatitis and the development of its systemic complications is suggested.  (+info)

Amylases are a group of enzymes that break down complex carbohydrates, such as starch and glycogen, into simpler sugars like glucose. There are two main types of amylases: salivary amylase and pancreatic amylase. Salivary amylase is produced by the salivary glands and is present in saliva. It begins the process of breaking down carbohydrates in the mouth, before they are further digested in the small intestine. Pancreatic amylase is produced by the pancreas and is released into the small intestine. It continues the process of breaking down carbohydrates into simpler sugars, which can then be absorbed by the body. Amylases are important for proper digestion and absorption of carbohydrates. Abnormal levels of amylases can indicate certain medical conditions, such as pancreatitis, salivary gland disorders, or certain types of cancer.

Alpha-amylases are a group of enzymes that break down complex carbohydrates, such as starch, into simpler sugars like glucose. They are produced by various organisms, including bacteria, fungi, plants, and animals, and are commonly used in the food industry to break down starches in grains and other crops to make them more easily digestible. In the medical field, alpha-amylases are often used as diagnostic tools to detect and monitor conditions that affect carbohydrate metabolism, such as diabetes and pancreatic insufficiency. They are also used in research to study the mechanisms of carbohydrate digestion and absorption. Alpha-amylases are sometimes used as a marker of pancreatic function, as the pancreas produces a specific type of alpha-amylase called pancreatic alpha-amylase. When the pancreas is not functioning properly, the levels of pancreatic alpha-amylase in the blood may be elevated. This can be an indication of conditions such as chronic pancreatitis or pancreatic cancer. Overall, alpha-amylases play an important role in carbohydrate metabolism and are useful tools in both the food industry and the medical field.

Pancreatitis is a medical condition characterized by inflammation of the pancreas, a gland located in the abdomen behind the stomach. The pancreas plays a crucial role in the digestive system by producing enzymes that help break down food and hormones that regulate blood sugar levels. There are two main types of pancreatitis: acute and chronic. Acute pancreatitis is a sudden and severe inflammation of the pancreas that usually lasts for a few days to a few weeks. It can be caused by a variety of factors, including excessive alcohol consumption, gallstones, infections, and certain medications. Symptoms of acute pancreatitis may include severe abdominal pain, nausea, vomiting, fever, and elevated levels of certain enzymes in the blood. Chronic pancreatitis is a long-term inflammation of the pancreas that can develop over time due to repeated episodes of acute pancreatitis, long-term alcohol abuse, or other factors. It can cause permanent damage to the pancreas, leading to problems with digestion and blood sugar control. Symptoms of chronic pancreatitis may include abdominal pain, weight loss, malnutrition, and diabetes. Treatment for pancreatitis depends on the severity and underlying cause of the condition. In some cases, hospitalization may be necessary to manage pain, prevent complications, and provide supportive care. In other cases, lifestyle changes such as quitting smoking and reducing alcohol consumption may be recommended to prevent future episodes. Medications and surgery may also be used to treat specific causes of pancreatitis, such as gallstones or infections.

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Isoamylase is an enzyme that is found in the pancreas, salivary glands, and small intestine. It is also produced by certain bacteria and fungi. In the medical field, isoamylase is often used as a diagnostic tool to help identify conditions such as pancreatitis, pheochromocytoma, and certain types of cancer. There are three main types of isoamylase: alpha-amylase, beta-amylase, and gamma-amylase. Alpha-amylase is the most common type and is found in the pancreas, salivary glands, and small intestine. Beta-amylase is found in the pancreas and small intestine, while gamma-amylase is found in the pancreas and liver. When levels of isoamylase in the blood or urine are elevated, it can be a sign of a problem with the pancreas or other organs. For example, high levels of isoamylase in the blood can be a sign of pancreatitis, while high levels in the urine can be a sign of pheochromocytoma or certain types of cancer.

Cholecystokinin (CCK) is a hormone that is produced by cells in the small intestine and the pancreas. It plays a role in regulating the digestive process by stimulating the release of digestive enzymes and bile from the pancreas and gallbladder, respectively. CCK also helps to slow down the movement of food through the small intestine, allowing more time for digestion and absorption of nutrients. In addition to its role in digestion, CCK has been found to have other functions in the body, including the regulation of appetite and the control of blood sugar levels.

Lipase is an enzyme that breaks down fats (lipids) into smaller molecules called fatty acids and glycerol. It is produced by various cells in the body, including pancreatic cells, and is important for the digestion and absorption of dietary fats. In the medical field, lipase is often measured in blood or stool samples to diagnose and monitor conditions related to fat metabolism, such as pancreatitis, biliary tract disease, and malabsorption syndromes. High levels of lipase in the blood or stool can indicate an acute pancreatitis, while low levels can suggest a deficiency in pancreatic function. Lipase is also used in medical research and drug development, as it plays a key role in the metabolism of lipids and the regulation of energy homeostasis. Additionally, lipase inhibitors are used in the treatment of obesity and type 2 diabetes, as they can help reduce the absorption of dietary fats and lower blood lipid levels.

In the medical field, starch refers to a type of carbohydrate that is found in plants, particularly in grains such as wheat, corn, and potatoes. Starch is a complex carbohydrate that is made up of long chains of glucose molecules. Starch is an important source of energy for the body and is broken down into glucose during digestion. It is also used in the production of various medical products, such as intravenous fluids, medications, and medical devices. In some cases, starch may be used as a thickening agent in medical products, such as eye drops or nasal sprays. It can also be used as a filler in certain medications to help with their texture or consistency. However, it is important to note that not all starches are created equal. Some types of starch, such as amylose, are more easily digested than others, such as amylopectin. Additionally, some people may have difficulty digesting certain types of starches, which can lead to digestive issues such as bloating or diarrhea.

Sincalide is a medication used in the medical field to help diagnose and treat certain conditions related to the pancreas and bile ducts. It is a synthetic version of a hormone called cholecystokinin (CCK), which is naturally produced by the body and helps to stimulate the release of bile from the liver and gallbladder. Sincalide is typically used in two main ways: 1. To diagnose conditions such as chronic pancreatitis, pancreatic cancer, and bile duct obstruction. In these cases, sincalide is injected into a vein and the patient's response to the medication is monitored. If the patient experiences symptoms such as abdominal pain or nausea, it may indicate that there is a problem with the pancreas or bile ducts. 2. To stimulate the release of bile in patients who have had their gallbladder removed (a condition known as cholecystectomy). In this case, sincalide is used to help prevent the development of a condition called postcholecystectomy syndrome, which can cause symptoms such as abdominal pain and nausea. Sincalide is generally considered safe and well-tolerated, although it can cause side effects such as abdominal pain, nausea, and diarrhea. It is important to note that sincalide should only be used under the supervision of a healthcare professional.

Salivary alpha-amylases are enzymes that are produced by the salivary glands and are found in saliva. They are responsible for breaking down complex carbohydrates, such as starch, into simpler sugars that can be easily absorbed by the body. Salivary alpha-amylases play an important role in the initial stages of digestion and are involved in the breakdown of food in the mouth. They are also used as a diagnostic tool in the medical field, as levels of salivary alpha-amylases can be elevated in certain medical conditions, such as pancreatitis, salivary gland disorders, and some types of cancer.

Trypsinogen is a precursor protein of trypsin, which is a digestive enzyme that plays a crucial role in the breakdown of proteins in the small intestine. Trypsinogen is produced in the pancreas and is secreted into the small intestine as an inactive form. Once it reaches the small intestine, it is activated by the enzyme chymotrypsin, which cleaves the inactive trypsinogen into active trypsin. Trypsin then cleaves proteins into smaller peptides and amino acids, which can be absorbed by the body and used for various functions. In the medical field, trypsinogen levels can be measured in blood or stool samples to diagnose and monitor conditions such as chronic pancreatitis, pancreatic cancer, and cystic fibrosis.

Chymotrypsinogen is a precursor protein that is produced in the pancreas and converted into the active enzyme chymotrypsin in the small intestine. Chymotrypsin is a protease enzyme that breaks down proteins into smaller peptides and amino acids. It plays an important role in the digestion of dietary proteins and is essential for proper nutrient absorption. In the medical field, chymotrypsinogen levels may be measured as part of diagnostic tests for pancreatic disorders, such as chronic pancreatitis or pancreatic cancer. Abnormal levels of chymotrypsinogen may indicate inflammation or damage to the pancreas.

Hyperamylasemia is a medical condition characterized by an abnormally high level of amylase in the blood. Amylase is an enzyme that is produced by the pancreas and salivary glands, and it is responsible for breaking down complex carbohydrates into simpler sugars. In normal circumstances, the level of amylase in the blood is relatively low and stable. However, in cases of hyperamylasemia, the level of amylase in the blood is significantly elevated, often due to damage or inflammation of the pancreas or salivary glands. Hyperamylasemia can be caused by a variety of medical conditions, including acute pancreatitis, chronic pancreatitis, pancreatic cancer, salivary gland disorders, and certain medications. It can also be a normal response to stress or physical activity. The diagnosis of hyperamylasemia typically involves measuring the level of amylase in the blood. Treatment depends on the underlying cause of the condition and may include medications, surgery, or lifestyle changes. In some cases, hyperamylasemia may resolve on its own without any treatment.

Bethanechol compounds are a class of drugs that are used to stimulate the contractions of smooth muscles in the body. They are primarily used to treat conditions such as urinary retention, constipation, and gastrointestinal disorders. Bethanechol works by activating muscarinic receptors in the smooth muscles, which leads to increased muscle contractions. It is available in both oral and injectable forms.

Salivary proteins and peptides are molecules that are secreted by the salivary glands and are present in saliva. They play important roles in various aspects of oral health and function, including lubrication of the mouth, protection against bacterial and viral infections, and digestion of food. Some of the major classes of salivary proteins and peptides include mucins, amylase, lipase, lysozyme, lactoferrin, and histatins. Mucins are large, complex glycoproteins that help to lubricate and protect the oral mucosa, while amylase and lipase are digestive enzymes that break down carbohydrates and fats in food. Lysozyme is an antimicrobial protein that helps to protect against bacterial infections, while lactoferrin and histatins have antimicrobial and anti-inflammatory properties. Abnormal levels or function of salivary proteins and peptides can be associated with various oral and systemic diseases, such as dry mouth, periodontal disease, and cancer. Therefore, the study of salivary proteins and peptides is an important area of research in the medical field.

Secretin is a hormone produced by the cells of the small intestine. It is released in response to the presence of food in the small intestine and plays a role in regulating the digestive process. Secretin stimulates the pancreas to release bicarbonate, which helps to neutralize stomach acid and protect the lining of the small intestine. It also stimulates the gallbladder to release bile, which helps to break down fats in the small intestine. In addition to its role in digestion, secretin has been studied for its potential therapeutic uses in a variety of medical conditions, including irritable bowel syndrome, chronic pancreatitis, and certain types of cancer.

Maltose is a disaccharide sugar composed of two molecules of glucose joined together by a glycosidic bond. It is commonly found in grains, especially barley, and is often used as a sweetener in food and beverages. In the medical field, maltose is used as a source of energy for the body and is sometimes used as a diagnostic tool to test for certain medical conditions, such as lactose intolerance. It is also used in the production of certain medications and as a food additive.

In the medical field, an acute disease is a condition that develops suddenly and progresses rapidly over a short period of time. Acute diseases are typically characterized by severe symptoms and a high degree of morbidity and mortality. Examples of acute diseases include pneumonia, meningitis, sepsis, and heart attacks. These diseases require prompt medical attention and treatment to prevent complications and improve outcomes. In contrast, chronic diseases are long-term conditions that develop gradually over time and may persist for years or even decades.

Pancreatic diseases refer to a group of medical conditions that affect the pancreas, a gland located in the abdomen behind the stomach. The pancreas plays a vital role in the digestive and endocrine systems, producing enzymes that help break down food and hormones that regulate blood sugar levels. Pancreatic diseases can be classified into two main categories: exocrine pancreatic diseases and endocrine pancreatic diseases. Exocrine pancreatic diseases affect the pancreas' ability to produce digestive enzymes, leading to malabsorption of nutrients and digestive problems. Examples of exocrine pancreatic diseases include chronic pancreatitis, cystic fibrosis, and pancreatic cancer. Endocrine pancreatic diseases affect the pancreas' ability to produce hormones, leading to imbalances in blood sugar levels. Examples of endocrine pancreatic diseases include type 1 diabetes, type 2 diabetes, and pancreatic neuroendocrine tumors. Pancreatic diseases can be challenging to diagnose and treat, as they often present with non-specific symptoms and can affect multiple organ systems. Treatment options depend on the specific disease and may include medications, surgery, or other interventions.

Pancreatic alpha-amylases are a group of enzymes that are produced by the pancreas and are responsible for breaking down complex carbohydrates, such as starch, into simpler sugars. These enzymes are secreted into the small intestine, where they help to digest the carbohydrates in the food we eat. There are two main types of pancreatic alpha-amylases: pancreatic alpha-amylase 1 and pancreatic alpha-amylase 2. Pancreatic alpha-amylase 1 is responsible for breaking down larger starch molecules, while pancreatic alpha-amylase 2 is responsible for breaking down smaller starch molecules. Pancreatic alpha-amylases are important for proper digestion and absorption of carbohydrates, and deficiencies in these enzymes can lead to malabsorption of carbohydrates and other digestive problems.

In the medical field, a trisaccharide is a type of carbohydrate that is composed of three monosaccharide units. Trisaccharides are often found in complex carbohydrates, such as starches and glycogen, and they can also be found in some dietary fibers. They are an important source of energy for the body and are also involved in a variety of biological processes, including the regulation of blood sugar levels and the immune response. Trisaccharides can be further broken down into smaller units by enzymes in the digestive system, allowing the body to absorb and utilize the energy they provide.

Carbachol is a medication that is used in the medical field to treat certain conditions such as glaucoma, irritable bowel syndrome, and urinary incontinence. It is a cholinergic agonist, which means that it works by stimulating the action of a neurotransmitter called acetylcholine in the body. Acetylcholine is involved in a wide range of bodily functions, including muscle contraction, digestion, and the regulation of the heart rate and blood pressure. By stimulating the action of acetylcholine, carbachol can help to relax muscles, increase the production of digestive juices, and slow down the heart rate and blood pressure. It is usually administered as an eye drop for glaucoma, as a suppository for irritable bowel syndrome, or as an injection for urinary incontinence.

Liver cirrhosis is a chronic liver disease characterized by the replacement of healthy liver tissue with scar tissue, leading to a loss of liver function. This scarring, or fibrosis, is caused by a variety of factors, including chronic alcohol abuse, viral hepatitis, non-alcoholic fatty liver disease, and autoimmune liver diseases. As the liver becomes increasingly damaged, it becomes less able to perform its many functions, such as filtering toxins from the blood, producing bile to aid in digestion, and regulating blood sugar levels. This can lead to a range of symptoms, including fatigue, weakness, abdominal pain, jaundice, and confusion. In advanced cases, liver cirrhosis can lead to liver failure, which can be life-threatening. Treatment options for liver cirrhosis depend on the underlying cause and may include lifestyle changes, medications, and in some cases, liver transplantation.

Liver Cirrhosis, Biliary refers to a condition where the liver becomes scarred and damaged due to chronic inflammation and scarring of the bile ducts. Bile ducts are responsible for carrying bile, a fluid produced by the liver, from the liver to the small intestine. The most common cause of liver cirrhosis, biliary is chronic inflammation of the bile ducts, which can be caused by various factors such as infections, autoimmune disorders, and inherited genetic conditions. Other causes include liver damage due to alcohol, viral hepatitis, and exposure to toxins. Symptoms of liver cirrhosis, biliary may include jaundice (yellowing of the skin and eyes), abdominal pain, fatigue, loss of appetite, and weight loss. In severe cases, it can lead to liver failure, which can be life-threatening. Treatment for liver cirrhosis, biliary depends on the underlying cause and the severity of the condition. In some cases, medications or surgery may be used to treat the underlying cause. In other cases, supportive care may be provided to manage symptoms and prevent complications such as infections and bleeding. In severe cases, a liver transplant may be necessary.

Liver Cirrhosis, Alcoholic is a chronic liver disease that occurs as a result of long-term excessive alcohol consumption. It is characterized by the scarring and hardening of the liver tissue, which can lead to liver failure and other serious complications. The liver is responsible for filtering toxins from the blood, producing bile to aid in digestion, and regulating various metabolic processes in the body. When the liver is damaged by excessive alcohol consumption, it becomes unable to perform these functions properly, leading to a buildup of toxins in the body and the development of cirrhosis. Symptoms of liver cirrhosis, alcoholic may include fatigue, weakness, abdominal pain, swelling in the legs and ankles, jaundice (yellowing of the skin and eyes), and confusion. In advanced stages, the disease can lead to liver failure, which can be life-threatening. Treatment for liver cirrhosis, alcoholic typically involves stopping alcohol consumption and addressing any underlying medical conditions that may be contributing to the disease. In some cases, medications or liver transplantation may be necessary to manage symptoms and prevent further liver damage.

Liver Cirrhosis, Experimental refers to a condition in which the liver becomes scarred and damaged due to various experimental procedures or treatments. This can occur in laboratory animals or humans who are undergoing medical research or clinical trials. Experimental liver cirrhosis can be induced by various methods, such as administering toxins, viruses, or other substances that cause liver damage. The purpose of such experiments is to study the pathophysiology of liver disease and to develop new treatments or therapies. The severity and extent of liver damage in experimental liver cirrhosis can vary depending on the type and duration of the experimental procedure. In some cases, the liver damage may be reversible, while in others, it may be irreversible and lead to liver failure or death. It is important to note that experimental liver cirrhosis is a controlled and regulated process that is conducted under strict ethical guidelines to minimize harm to the animals or humans involved.

Achlorhydria is a medical condition characterized by the absence or significantly reduced production of hydrochloric acid in the stomach. Hydrochloric acid is a digestive enzyme that plays a crucial role in the breakdown of proteins, fats, and carbohydrates in the stomach. Achlorhydria can be caused by a variety of factors, including damage to the stomach lining, certain medications, autoimmune disorders, and genetic mutations. It can also be a side effect of certain medical treatments, such as radiation therapy or chemotherapy. Symptoms of achlorhydria may include heartburn, nausea, vomiting, bloating, and difficulty digesting certain foods. In severe cases, achlorhydria can lead to malnutrition and other complications. Treatment for achlorhydria typically involves dietary changes and the use of medications to help with digestion and absorption of nutrients. In some cases, surgery may be necessary to repair damage to the stomach lining or to remove tumors that are causing the condition.

Both α-amylase and β-amylase are present in seeds; β-amylase is present in an inactive form prior to germination, whereas α- ... In human physiology, both the salivary and pancreatic amylases are α-amylases. The α-amylase form is also found in plants, ... The γ-amylase has the most acidic optimum pH of all amylases because it is most active around pH 3. They belong to a variety of ... All amylases are glycoside hydrolases and act on α-1,4-glycosidic bonds. The α-amylases (EC 3.2.1.1 ) (CAS 9014-71-5) ( ...
The optimum pH for β-amylase is 4.0-5.0 They belong to Glycoside hydrolase family 14. Amylase Alpha-amylase Rejzek M, Stevenson ... "Amylase, Alpha" , I.U.B.: 3.2.1.11,4-α-D-Glucan glucanohydrolase. "Amylase, Alpha" , I.U.B.: 3.2.1.11,4-α-D-Glucan ... β-Amylase (EC 3.2.1.2, saccharogen amylase, glycogenase) is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. It ... β-amylase is present in an inactive form prior to seed germination. Many microbes also produce amylase to degrade extracellular ...
See amylase for more uses of the amylase family in general. α-Amylase has exhibited efficacy in degrading polymicrobial ... Medical laboratories will usually measure either pancreatic amylase or total amylase. If only pancreatic amylase is measured, ... In humans, all amylase isoforms link to chromosome 1p21 (see AMY1A). Amylase is found in saliva and breaks starch into maltose ... The alpha-Amylase Protein alpha-Amylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) This article ...
In molecular biology, alpha-amylase inhibitor (or α-...) is a protein family which inhibits mammalian alpha-amylases ... The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme. The crystal ... This family of inhibitors has no action on plant and microbial alpha amylases. A crystal structure has been determined for ... König V, Vértesy L, Schneider TR (October 2003). "Structure of the alpha-amylase inhibitor tendamistat at 0.93 A". Acta ...
This is a list of amylase-induced fermentations. Saliva can be used as a source of the enzyme amylase to break down complex ... Amylase-induced fermented drinks are often made from cassava. Fermented beverage cauim chicha: Throughout the Amazon Basin, ... Articles needing additional references from September 2014, All articles needing additional references, Amylase induced ...
Sherman, H. C., & Thomas, A. W. (1915). Studies on amylases. VIII. The influence of certain acids and salts upon the activity ... Thomas, A. W. (1917). A noteworthy effect of bromides upon the action of malt amylase. Journal of the American Chemical Society ... Isoelectric point of malt amylase. Journal of the American Chemical Society, 46, 1711-6. Thomas, A. W., & Kelly, M. W. (1925). ... Influence of hydrogen-ion concentration upon enzymatic activity of three typical amylases. Journal of the American Chemical ...
Other names in common use include amylase III, and 1,4-alpha-glucan:1,4-alpha-glucan 4-alpha-glucosyltransferase. Nebinger P ( ... Characterization of amylases". Biological Chemistry Hoppe-Seyler. 367 (3): 169-76. doi:10.1515/bchm3.1986.367.1.169. PMID ... Nebinger P (March 1986). "Separation and characterization of four different amylases of Entamoeba histolytica. II. ... March 1986). "Separation and characterization of four different amylases of Entamoeba histolytica. I. Purification and ...
Hanes, C.S. (1932). "Studies on plant amylases. I. The effect of starch concentration upon the velocity of hydrolysis by the ... amylase of germinated barley". Biochem. J. 26 (2): 1406-1421. doi:10.1042/bj0261406. PMC 1261052. PMID 16744959. Eadie, G. S. ( ...
doi:10.1016/S0021-9258(18)44843-0. Hanes, C.S. (1932). "Studies on plant amylases. I. The effect of starch concentration upon ... "Exploring the inhibitory mechanism of p-coumaric acid on α-amylase via multi-spectroscopic analysis, enzymatic inhibition assay ... the velocity of hydrolysis by the amylase of germinated barley". Biochem. J. 26 (2): 1406-1421. doi:10.1042/bj0261406. PMC ...
The different classes of amylases are α-amylases, β-amylases, and glucoamylases. The α-amylases hydrolyze starch by randomly ... Amylase breaks down carbohydrates into mono- and disaccharides, so a starch agar must be used for this assay. Once the bacteria ... In humans, amylases are secreted by the pancreas and salivary glands, with both sources of the enzyme required for complete ... Since iodine binds to starch but not its digested by-products, a clear area will appear where the amylase reaction has occurred ...
Amylase". Journal of Fish Biology. 14 (6): 565-572. doi:10.1111/j.1095-8649.1979.tb03556.x. v t e (Articles with short ...
It is composed of amylase, lipase and protease. This mixture is used to treat conditions in which pancreatic secretions are ... "Pancrelipase Amylase; Pancrelipase Lipase; Pancrelipase Protease - Drug Usage Statistics". ClinCalc. Retrieved 7 October 2022. ... Pancreatic enzymes, also known as pancreases or pancrelipase and pancreatin, are commercial mixtures of amylase, lipase, and ... The trypsin found in pancreatin works to hydrolyze proteins into oligopeptides; amylase hydrolyzes starches into ...
In cases of pancreatitis, there may be elevated levels of lipase or amylase, an enzyme found in saliva and the pancreas. Mumps ... "Amylase Test". Lab Tests Online. Archived from the original on 29 March 2009. Retrieved 30 October 2020. "Mumps Clinical ... Skrha J, Stepan J, Sixtova E (October 1979). "Amylase isoenzymes in mumps". Eur J Pediatr. 132 (2): 99-105. doi:10.1007/ ...
Reasons for false positive elevated serum amylase include salivary gland disease (elevated salivary amylase), bowel obstruction ... Serum amylase may be normal (in 10% of cases) for cases of acute or chronic pancreatitis (depleted acinar cell mass) and ... Lin XZ, Wang SS, Tsai YT, Lee SD, Shiesh SC, Pan HB, Su CH, Lin CY (February 1989). "Serum amylase, isoamylase, and lipase in ... Another study found that the amylase could add diagnostic value to the lipase, but only if the results of the two tests were ...
"Reference range (amylase)". GPnotebook. Ageno W, Finazzi S, Steidl L, et al. (2002). "Plasma measurement of D-dimer levels for ...
"Plant α-amylase inhibitors and their interaction with insect α-amylases: Structure, function and potential for crop protection ... Some plant defensins have also been identified as enzyme inhibitors of α-amylase or trypsin. It is believed that these are ... Richardson M, Bloch Jr C (1991). "A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds or ... "Novel insights on the mechanism of action of α-amylase inhibitors from the plant defensin family". Proteins: Structure, ...
"Amylases and bread firming - an integrated view". Journal of Cereal Science. Special Section: Enzymes in Grain Processing. 50 ( ...
Maltogenic amylases from Bacillus stearothermophilus, Thermus sp. and Geobacillus thermoleovorans are able to degrade acarbose ... Glucan 1,4-alpha-maltohydrolase (EC 3.2.1.133, maltogenic alpha-amylase, 1,4-alpha-D-glucan alpha-maltohydrolase) is an enzyme ... Diderichsen B, Christiansen L (1988). "Cloning of a maltogenic α-amylase from Bacillus stearothermophilus". FEMS Microbiol. ... April 1998). "Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose ...
This heating process activates enzymes called amylases. The shape of these enzymes, their active site, gives them the unique ...
... enzymes such as amylase; and prostaglandins. Its consistency is determined by the influence of the hormones estrogen and ...
nov., a amylase producing bacterium isolated from a hot spring". Systematic and Applied Microbiology. 28 (5): 415-20. doi: ... Caldimonas taiwanensis produces amylase. Parte, A.C. "Caldimonas". LPSN. "Caldimonas taiwanensis Taxon Passport - StrainInfo". ...
... produces amylase. LPSN lpsn.dsmz.de Deutsche Sammlung von Mikroorganismen und Zellkulturen [1] ... Smith, Michael R.; Zahnley, James C. (2 June 2005). "Production of amylase by Arthrobacter psychrolactophilus". Journal of ... Smith, Michael R.; Zahnley, James C. (19 August 2005). "Characteristics of the amylase of Arthrobacter psychrolactophilus". ...
The human AMY1C gene encodes the protein Amylase, alpha 1C (salivary). Amylases are secreted proteins that hydrolyze 1,4-alpha- ... This gene encodes an amylase isoenzyme produced by the salivary gland. See also Amylase § Evolution. GRCh38: Ensembl release 89 ... The human genome has a cluster of several amylase genes that are expressed at high levels in either the salivary gland or ... "Entrez Gene: Amylase, alpha 1C (salivary)". Retrieved 2013-02-14. [provided by RefSeq, Jul 2008]. ##RefSeq-Attributes-START## ...
The midgut also contains amylases, roteases and upases. The narrow cells in its reservoir have little to no function in ... which includes proteases and amylases that function as an extraintestinal digestion of solid food. ...
An elevated amylase level, usually > 1,000 IU/L, with protein levels over 3.0 g/dL is diagnostic. Serum amylase is often ...
Fischer worked on α-amylase. After his PhD, Fischer went to the United States in 1950 for postdoctoral research. He was ...
Beta-amylase is present in certain bacteria as well as in plants. Three highly conserved sequence regions are found in all ... Beta-amylase is an enzyme that hydrolyzes 1,4-alpha-glucosidic linkages in starch-type polysaccharide substrates so as to ... The 3D structure of a complex of soybean beta-amylase with an inhibitor (alpha-cyclodextrin) has been determined to 3.0A ... Glycoside hydrolase family 14 CAZY GH_14 comprises enzymes with only one known activity; beta-amylase (EC 3.2.1.2). A Glu ...
Amylase DNA polymerase Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter (2002). " ...
Chao SE, Scandalios JG (1972). "Developmentally dependent expression of tissue specific amylases in maize". Molecular & General ...
Since these tests specifically target amylase, confirmatory tests can not be done considering amylase can be found in other ... RSID tests have also been made in order to detect alpha-amylase, but they are not always reliable because there can be a lot of ... A presumptive test to detect saliva is the alpha-amylase test also known as the Phadebas Test. This detection technique is ... If saliva is present, then the alpha-amylase breaks down the starch, creating a clear coloured circle around where the sample ...
Amylase is an enzyme that helps digest carbohydrates. It is produced mainly in the pancreas and the glands that make saliva. ... This is a test that measures the amount of amylase in urine. ... Increased urine amylase levels may be a sign of:. *Acute ... This is a test that measures the amount of amylase in urine. Amylase is an enzyme that helps digest carbohydrates. It is ... An increased amount of amylase in the urine is called amylasuria. ...
The reference range for amylase is as follows: Serum test: Normal is 40-140 U/L Urine Test: Normal is 24-400 U/L ... Alpha amylase is of salivary or pancreatic origin and referred to as S-type or P-type amylase, respectively. Pancreatic amylase ... Urine amylase increases in proportion to serum amylase and remains elevated for several days after serum amylase has been ... Most elevations in serum amylase are due to increased rates of amylase entry into the blood stream, decreased rates of ...
Pancreatic Amylase measurements are primarily used for the diagnosis and treatment of pancreatitis as well as pancreatic ... What is Pancreatic Amylase assay used for?. Amylase is an enzyme present in pancreatic fluids within the small intestine. It is ... Amylase levels rise quickly at the start of a pancreatitis attack and fall after around 2 days. Elevated levels may also be ... Amylase measurements are used primarily for the diagnosis and treatment of pancreatitis (severe inflammation of the pancreas) ...
5th International Infogest Webinar on Food Digestion: Digestive amylases and starch digestion. 11 January 2021 Type Event ... 5th International Infogest Webinar on Food Digestion: Digestive amylases and starch digestion ...
N/A PuraDymes Amylase formula is a unique blend of high potency enzymes that catalyze the breakdown of starch into sugars and ... PuraDymes Amylase formula is a unique blend of high potency enzymes that catalyze the breakdown of starch into sugars and aid ... Gluco Amylase- 40mg (160 AGU). *Puradyme Cofactor Whole Food Blend-100mg. Quinoa Sprouts, Fennel Seed, Rose Hips (Rosa canina)( ...
Amylase, α- (9CI); FD Super; Aquazyme SD-L; Spezyme LT-300; Timextra; Palkodex; Amylex A3; Amylase THC 250; Speedase M; Bioferm ... Amylase, α- (9CI); FD Super; Aquazyme SD-L; Spezyme LT-300; Timextra; Palkodex; Amylex A3; Amylase THC 250; Speedase M; Bioferm ...
Amylase induction during seed germination in isoproturon susceptible and resistant biotypes of Phalaris minor Retz. ... Higher amylase activity is observed in the initial hours of imbibition in the resistant biotype. In the susceptible biotype it ...
The reference range for amylase is as follows: Serum test: Normal is 40-140 U/L Urine Test: Normal is 24-400 U/L ... Alpha amylase is of salivary or pancreatic origin and referred to as S-type or P-type amylase, respectively. Pancreatic amylase ... Urine amylase increases in proportion to serum amylase and remains elevated for several days after serum amylase has been ... Most elevations in serum amylase are due to increased rates of amylase entry into the blood stream, decreased rates of ...
The reference range for amylase is as follows: Serum test: Normal is 40-140 U/L Urine Test: Normal is 24-400 U/L ... Alpha amylase is of salivary or pancreatic origin and referred to as S-type or P-type amylase, respectively. Pancreatic amylase ... Urine amylase increases in proportion to serum amylase and remains elevated for several days after serum amylase has been ... Most elevations in serum amylase are due to increased rates of amylase entry into the blood stream, decreased rates of ...
Effect of Alcohol Withdrawl on Glutathione S-transferase, Total Antioxidant Capacity and Amylase in Blood and Saliva of Alcohol ...
... amylase) (EC 3.2.1.1) is an endo-amylolytic enzyme that plays an important role in seed germination in wheat. However, ... Alpha amylase (?-amylase) (EC 3.2.1.1) is an endo-amylolytic enzyme that plays an important role in seed germination in wheat. ... However, excessive ?-amylase in post-harvest wheat grains has a negative effect on wheat yield and end-products quality. A wide ... range of studies have been carried out on wheat alpha amylase due to its important biological roles in post-harvest spouting. ...
Amylase. The starch is converted to malt sugar and dextrins by amylase. Not all dextrins are converted to malt sugar, thereby ...
Our proven Amylase Enzyme is designed for home brewing. Great for light and low carb beers. Shop now. ... Order premium Amylase Enzyme from Craft a Brew. ... Alpha Amylase Enzyme is ideal for use in beers that dont have ... Amylase Enzyme helps you brew your best light and low carb beers. This helpful ingredient increases a beers fermentability by ...
Hence the activity of Alfa-amylase was measured in terms of mg maltose released during first five minutes. Alfa-amylase showed ... The immobilized Alfa-amylase (prepared at pH 8.3) was stable on storage for a period of 3 weeks at 4 0 C in 0.4M phosphate ... Alfa-amylase was coupled to cyanogen bromide activated Sephadex G200 at pH8.3 and 7.0. Coupling of the enzyme led to further ... The activities of the Alfa-amylases immobilized at pH 8.3 and 7.0 were, 0.75 percent and 0.52 percent of the total soluble Alfa ...
This Amylase Enzyme Formula helps brewers convert starches into sugar, preventing starch haze in beer. For a 5 gallon batch, ... This Amylase Enzyme Formula helps brewers convert starches into sugar, preventing starch haze in beer. For a 5 gallon batch, ... This Amylase Enzyme Formula helps brewers convert starches into sugar, preventing starch haze in beer. For a 5 gallon batch, ...
Phadebas® , [email protected] , © Phadebas AB , Corporate identity number: 559136-9847 ...
Be the first to review "Alpha-Amylase Enzyme" Cancel reply. Your email address will not be published. Required fields are ... Thermostable powdered alpha-amylase enzyme for hydrolysis of long-chain starch molecules into short-chain dextrins. For use in ...
Alpha-Amylase is a bacterial-derived enzyme which breaks down starch into dextrins and simple sugars during mashing. Good up to ...
... Fast and Free Shipping ... Amylase #3 - 90 caps by Ness Enzymes. Amylase by Ness Enzymes ... Decrease Quantity of Amylase #3 - 90 caps Increase Quantity of Amylase #3 - 90 caps ... Amylase (formula 3) also can be used with any NESS™ product containing multiple enzymes when more amylase is necessary. *,/div ... Amylase (formula 3) also can be used with any NESS™ product containing multiple enzymes when more amylase is necessary. * ...
... amylase by SmF was observed at 250C in Nutrient Broth (270 U/ml). The optimum production of ?-amylase by SmF was observed at ... amylase by SmF was observed at 250C in Nutrient Broth (270 U/ml). The optimum production of ?-amylase by SmF was observed at ... The production of ?-amylases has been thoroughly investigated and observed that it was affected by a variety of physiochemical ... The production of ?-amylases has been thoroughly investigated and observed that it was affected by a variety of physiochemical ...
Usage varies. 1tsp. Breaks 1,4 linkage in starch during liquefication, producing dextrin and a small amout of maltose.. Leaves 1,6 links, therefore self-limiting. Use if you have a starch problem in storage, or in light beers. ...
3. Amylase and starch tolerance. Although there are certainly exceptions, meat-free diets tend to be higher in carbohydrates ... Although the amylase issue is relevant to anyone with a mouth, plant-based diets centered on grains, legumes, and tubers (like ... Not surprisingly, low amylase producers have a heightened risk of metabolic syndrome and obesity when eating standard high ... But for someone with the metabolic machinery to crank out plenty of amylase, handling a high carb, plant-based diet might be a ...
Effect Of Temperature On Amylase. 1167 Words , 5 Pages. The concentration of the Amylase was kept at 1% at at times throughout ... Bio Chem: Lab Report Of Amylase In Enzyme. 916 Words , 4 Pages. Bio Chem lab Report 04 Enzyme Biochemistry Group Member: Chan ... Bio Chem: Lab Report Of Amylase In Enzyme. 916 Words , 4 Pages ... amylase from saliva, 0.5M HCl solution, 0.5M NaOH solution and ...
Amylase Manufacturers and Factory. We accept OEM custom products all made in China. ... The α-amylase is prepared by deep fermentation of bacillus spp. It can hydrolyze amylose and amylopectin to produce dextrins ... 3. The alpha amylase enzyme activity can be maintained up to 90% for 6 months when stored at room temperature. ... 2. The use of amylase in the production of alcohol and brewing industry can make the enzymatic activity evenly distributed ...
What happens if serum amylase is high?. If your results show an abnormal level of amylase in your blood or urine, it may mean ... What is considered a high level of amylase?. The normal range for adults for amylase in a blood sample is 30 to 110 units per ... Why does serum amylase increase in pancreatitis?. It is thought that an initial insult to the pancreas causes the premature ... High amylase. *Acute or chronic pancreatitis. Acute or chronic pancreatitis occurs when the enzymes that help break down food ...
Both ?-amylase and the ?-amylase are the. present in the seeds; ?-amylase is the #present in an inactive form#before ... Amylase# an amylase is the enzyme that catalyzes the hydrolysis of. starch# into. sugars. Amylase is the present in human # ... amylases:. Amylases (EC 3.2.1.1) (CAS No. 9014-71-5). (alternative names: 1#4-?-D-glucan. glucanhydrolase#. glucogenase) are ... amylase (alpha amylase) to the hydrolyze #food starch into dis theaccharides and the tris the. accharides that other enzymes ...
  • Amylase is an enzyme that helps digest carbohydrates. (medlineplus.gov)
  • Plasma samples that have been anticoagulated with citrate or oxalate should be avoided because amylase is a calcium-containing enzyme and false low levels can be obtained with such specimens. (medscape.com)
  • Amylase is an enzyme produced in the pancreas and by the salivary glands that converts starches, glycogens, and related polysaccharides into simple and easily digested sugar. (medscape.com)
  • Amylase Enzyme helps you brew your best light and low carb beers. (craftabrew.com)
  • Alpha Amylase Enzyme is ideal for use in beers that don't have enough naturally occurring enzymes - usually in cases of high levels of adjuncts (like corn). (craftabrew.com)
  • Package contains 1 oz. of Alpha Amylase Enzyme. (craftabrew.com)
  • This Amylase Enzyme Formula helps brewers convert starches into sugar, preventing starch haze in beer. (urbanbrewers.com)
  • Alpha-Amylase is a bacterial-derived enzyme which breaks down starch into dextrins and simple sugars during mashing. (spokanebrewingsupply.com)
  • 3. The alpha amylase enzyme activity can be maintained up to 90% for 6 months when stored at room temperature. (starbiozyme.com)
  • Amylase# an amylase is the enzyme that catalyzes the hydrolysis of starch# into sugars. (lagas.org)
  • As a diastase# amylase was the# first enzyme dis thecovered# and the theolated (by Anselme Payen in 1833). (lagas.org)
  • Salivary cortisol , s- IgA and s-α- amylase concentrations were obtained by Enzyme-linked Immunosorbent Assay ( ELISA ). (bvsalud.org)
  • The 2 tests for amylase are serum and urine. (medscape.com)
  • Macroamylasemia is a condition of persistently elevated serum amylase activity with no apparent pancreatic disorder due to the formation of a large amylase-globulin complex, which is not excreted. (medscape.com)
  • Most elevations in serum amylase are due to increased rates of amylase entry into the blood stream, decreased rates of clearance or both. (medscape.com)
  • Serum amylase increases in 6-48 hrs of onset of acute pancreatitis but not in proportion to the severity of the disease and activity returns to normal in 3-5 days. (medscape.com)
  • Urine amylase increases in proportion to serum amylase and remains elevated for several days after serum amylase has been normalized. (medscape.com)
  • Other conditions in which determination of serum amylase is useful is to determine the effects of the removal of gallstones, and swelling and inflammation of the salivary/parotid glands. (medscape.com)
  • What happens if serum amylase is high? (corporatetaxratenow.com)
  • pancreatitis) or pancreatic duct is blocked, serum amylase levels increased. (corporatetaxratenow.com)
  • Why does serum amylase increase in pancreatitis? (corporatetaxratenow.com)
  • When inappropriately activated, trypsin causes pancreatic inflammation and auto-digestion, which can cause a release of amylase and lipase into the serum. (corporatetaxratenow.com)
  • and alanine aminotransferase {ALT} 138 U/L {normal: 7-56 U/L}). Although he reported no abdominal pain and the abdominal examination on admission was normal, serum amylase and lipase levels were elevated (amylase 226 U/L {normal: 30-110 U/L} and lipase 771 U/L {normal: 23-300 U/L}). Chest radiographs at the time of admission demonstrated perihilar interstitial infiltrates. (cdc.gov)
  • Studies using physiological [3, 4] and psychological stressors [5, 6] revealed increased activity of salivary alpha-amylase due to stress. (corporatetaxratenow.com)
  • Studies in humans have shown that alpha2-adrenergic [7] and beta-adrenergic [8] mechanisms are involved in increases of salivary alpha-amylase activity. (corporatetaxratenow.com)
  • Salivary alpha-amylase significantly increased in new patients while being seated in the dental chair. (bvsalud.org)
  • Amylase molecule from human saliva. (medscape.com)
  • The results of this study show that ferric chloride (FeCl3), magnesium chloride, ethylenediaminetetraacetic acid, and citric acid significantly decrease the α-amylase activity of saliva stains. (corporatetaxratenow.com)
  • Amylase is the present in human #saliva and the in some other mammals# where# the chemical process# of digestion begins. (lagas.org)
  • Amylase and lipase tests are used to detect pancreatitis. (corporatetaxratenow.com)
  • In this case, elevated amylase and lipase was probably due to acute gastritis and chronic alcoholism, considering the totally benign abdominal examination as well as the EGD findings. (corporatetaxratenow.com)
  • This is a test that measures the amount of amylase in urine. (medlineplus.gov)
  • An increased amount of amylase in the urine is called amylasuria. (medlineplus.gov)
  • Timed urine specimens can be obtained for urinary amylase and normalized to creatinine content. (medscape.com)
  • If your results show an abnormal level of amylase in your blood or urine, it may mean you have a disorder of the pancreas or other medical condition. (corporatetaxratenow.com)
  • Amylases are enzymes that catalyze the hydrolysis of amylopectin, amylose, glycogen, and their hydrolyzed products into simple and easily digestible sugars. (medscape.com)
  • The starch is converted to malt sugar and dextrins by amylase. (xn--lbryghus-44a.dk)
  • Foods that contain huge amounts# of starch but little# sugar# such as rice and the potatoes# can #obtain a slightly# sweet taste because they are the chewed because the #amylase degrades# some of the starch in the sugar. (lagas.org)
  • The pancreas# and the salivary gland the #produce amylase (alpha amylase) to the hydrolyze #food starch into dis theaccharides and the tris the accharides that other enzymes change into glucose to the offer energy to the the body. (lagas.org)
  • During the ripening of the# fruit# beta-amylase breaks# down the starch into# maltose# resulting in a sweet taste of the ripe fruit#. (lagas.org)
  • Pancreatic amylase is secreted by acinar cells of the pancreas and is tissue specific and more temperature labile than salivary amylase. (medscape.com)
  • High levels of amylase may indicate: Acute pancreatitis, a sudden and severe inflammation of the pancreas. (corporatetaxratenow.com)
  • Salivary amylase is synthesized by parotid, sweat, and lactating mammary glands. (medscape.com)
  • The proteins synthesized by parotid acinar cells are stored in large secretory granules whose composition includes α-amylase, leucine-rich parotid secretory protein (PSP), and proline-rich proteins (PRPs), in addition to multiple minor components 2-3 related to digestive and protective functions. (bvsalud.org)
  • Comparing Dental Stress in New Child Patients and Returning Patients Using Salivary Cortisol, Immunoglobulin-A and Alpha- Amylase. (bvsalud.org)
  • this study was aimed at comparing dental stress in children having their first dental visit to those returning for dental treatment using salivary biomarkers of stress including salivary cortisol (s- cortisol ), Immunoglobulin -A (s- IgA ) and alpha-amylase (s-α- amylase ). (bvsalud.org)
  • Plants and the some bacteria also produce amylase. (lagas.org)
  • Many microbes also produce amylases to the degrade extracellular starches. (lagas.org)
  • The #specific proteins of amylase are the #designated with dissimilar Greek letters. (lagas.org)
  • Alpha amylase is of salivary or pancreatic origin and referred to as S-type or P-type amylase, respectively. (medscape.com)
  • On agarose gel, the mobility of the less anionic isoenzyme corresponds to pancreatic amylase, while the more anionic band is salivary amylase. (medscape.com)
  • 1. In baking process, adding alpha amylase in the flour can increase fermentation, reduce the dough viscosity, increase sugar content of the dough, improve the taste, color and baking quality of bread, and extend the preservation period of baked foods. (starbiozyme.com)
  • The inhalable flour dust samples were further analyzed for alpha-amylase and wheat. (cdc.gov)
  • The ratio of amylase urinary clearance to creatinine clearance can be used in the diagnosis of acute and relapsing pancreatitis. (medscape.com)
  • How high is amylase in pancreatitis? (corporatetaxratenow.com)
  • Koh D, Ng V, Naing L. Alpha amylase as a salivary biomarker of acute stress of venepuncture from periodic medical examinations. (medscape.com)
  • These 30ml Alpha Amylase with Pepsin Drops are the perfect combination of Alpha amylase and Pepsin. (tucsonpharma.in)
  • In addition, these 30ml Alpha Amylase with Pepsin Drops are also used for effectively treating dyspepsia (indigestion), flatulence (gas), loss of appetite, burping, and abdominal distention. (tucsonpharma.in)
  • Higher amylase activity is observed in the initial hours of imbibition in the resistant biotype. (niscair.res.in)
  • 2. The use of amylase in the production of alcohol and brewing industry can make the enzymatic activity evenly distributed during fermentation, improve the saccharification, alcohol yield and yeast growth. (starbiozyme.com)
  • Returning patients had higher s-α- amylase (p=0.001) and s- IgA (p=0.016) compared to new patients . (bvsalud.org)
  • 3. In feed industry, adding amylase in combination with semicellulase can improve the digestibility of corn, increase the value of feed utilization, and reduce the production cost. (starbiozyme.com)
  • Each small capsule contains enzymes like amylase, lipase, cellulase and protease to break down macronutrients (carbohydrates, fats and protein, plus fiber) along with those hard-to-digest foods. (enzymedica.com)
  • EPI also results in a pancreatic shortage of enzymes such as amylase and protease, which help digest carbohydrates and protein. (healthline.com)
  • Amylases are enzymes that catalyze the hydrolysis of amylopectin, amylose, glycogen, and their hydrolyzed products into simple and easily digestible sugars. (medscape.com)
  • Enzymes like Amylase and Cellulase are frequently used in the textile industry to achieve certain characteristics of the fabric. (phadebas.com)
  • In this article, Anfinsen, et al, reported that while trying to study the factors that influenced protein thermostability, or the ability to remain stable at relatively high temperatures, they had cloned a gene from the hyperthermophilic bacterium Pyrococcus furiosus encoded with a highly thermostable alpha-amylase and expressed it in Escherichia Coli. (nih.gov)
  • Alpha amylase is of salivary or pancreatic origin and referred to as S-type or P-type amylase, respectively. (medscape.com)
  • Pancreatic amylase is secreted by acinar cells of the pancreas and is tissue specific and more temperature labile than salivary amylase. (medscape.com)
  • Salivary amylase is synthesized by parotid, sweat, and lactating mammary glands. (medscape.com)
  • On agarose gel, the mobility of the less anionic isoenzyme corresponds to pancreatic amylase, while the more anionic band is salivary amylase. (medscape.com)
  • Effects of Exposure to GSM Mobile Phone Base Station Signals on Salivary Cortisol, Alpha-Amylase, and Immunoglobulin A med. (emf-portal.org)
  • To test whether exposure to radiofrequency electromagnetic fields emitted by mobile phone base stations may have effects on salivary alpha- amylase , immunoglobulin A , and cortisol levels in human subjects . (emf-portal.org)
  • However, macroamylasemia can look similar to acute pancreatitis , which also causes high levels of amylase in the blood. (mountsinai.org)
  • Determination of alpha-amylase inhibitor activity of phaseolamin from kidney bean (Phaseolus vulgaris) in dietary supplements by HPAEC-PAD. (nih.gov)
  • However they are often annotated in the NCBI protein database as the DUF1551 or PF04314 family, alpha-amylase catalytic proteins, members of the Phenol_MetA-deg (MetA-pathway of phenol degradation) superfamily, signal peptide proteins and porins. (tcdb.org)
  • The ratio of amylase urinary clearance to creatinine clearance can be used in the diagnosis of acute and relapsing pancreatitis. (medscape.com)
  • The invention relates to rabbit antisera raised against purified human chymotrypsin and amylase. (nih.gov)