Amylases
Pancreas
Parotid Gland
alpha-Amylases
Pancreatitis
Ceruletide
Saliva
Isoamylase
Cholecystokinin
Pancreatic Juice
Lipase
Starch
Sincalide
Trypsinogen
Chymotrypsinogen
Hyperamylasemia
Pancreas, Exocrine
Bethanechol Compounds
Salivary Proteins and Peptides
Secretory Rate
Secretin
Maltose
Clinical Enzyme Tests
Pancreatic alpha-Amylases
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 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.
The parotid gland is the largest of the major salivary glands. It is a bilobed, accessory digestive organ that secretes serous saliva into the mouth via the parotid duct (Stensen's duct), located near the upper second molar tooth. The parotid gland is primarily responsible for moistening and lubricating food to aid in swallowing and digestion.
Anatomically, the parotid gland is located in the preauricular region, extending from the zygomatic arch superiorly to the angle of the mandible inferiorly, and from the masseter muscle anteriorly to the sternocleidomastoid muscle posteriorly. It is enclosed within a fascial capsule and has a rich blood supply from the external carotid artery and a complex innervation pattern involving both parasympathetic and sympathetic fibers.
Parotid gland disorders can include salivary gland stones (sialolithiasis), infections, inflammatory conditions, benign or malignant tumors, and autoimmune diseases such as Sjögren's syndrome.
Alpha-amylases are a type of enzyme that breaks down complex carbohydrates, such as starch and glycogen, into simpler sugars like maltose, maltotriose, and glucose. These enzymes catalyze the hydrolysis of alpha-1,4 glycosidic bonds in these complex carbohydrates, making them more easily digestible.
Alpha-amylases are produced by various organisms, including humans, animals, plants, and microorganisms such as bacteria and fungi. In humans, alpha-amylases are primarily produced by the salivary glands and pancreas, and they play an essential role in the digestion of dietary carbohydrates.
Deficiency or malfunction of alpha-amylases can lead to various medical conditions, such as diabetes, kidney disease, and genetic disorders like congenital sucrase-isomaltase deficiency. On the other hand, excessive production of alpha-amylases can contribute to dental caries and other oral health issues.
Pancreatitis is a medical condition characterized by inflammation of the pancreas, a gland located in the abdomen that plays a crucial role in digestion and regulating blood sugar levels. The inflammation can be acute (sudden and severe) or chronic (persistent and recurring), and it can lead to various complications if left untreated.
Acute pancreatitis often results from gallstones or excessive alcohol consumption, while chronic pancreatitis may be caused by long-term alcohol abuse, genetic factors, autoimmune conditions, or metabolic disorders like high triglyceride levels. Symptoms of acute pancreatitis include severe abdominal pain, nausea, vomiting, fever, and increased heart rate, while chronic pancreatitis may present with ongoing abdominal pain, weight loss, diarrhea, and malabsorption issues due to impaired digestive enzyme production. Treatment typically involves supportive care, such as intravenous fluids, pain management, and addressing the underlying cause. In severe cases, hospitalization and surgery may be necessary.
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.
Saliva is a complex mixture of primarily water, but also electrolytes, enzymes, antibacterial compounds, and various other substances. It is produced by the salivary glands located in the mouth. Saliva plays an essential role in maintaining oral health by moistening the mouth, helping to digest food, and protecting the teeth from decay by neutralizing acids produced by bacteria.
The medical definition of saliva can be stated as:
"A clear, watery, slightly alkaline fluid secreted by the salivary glands, consisting mainly of water, with small amounts of electrolytes, enzymes (such as amylase), mucus, and antibacterial compounds. Saliva aids in digestion, lubrication of oral tissues, and provides an oral barrier against microorganisms."
Isoamylase is not a medical term per se, but rather a biochemical term used to describe an enzyme. Medically, it may be relevant in the context of certain medical conditions or treatments that involve carbohydrate metabolism. Here's a general definition:
Isoamylase (EC 3.2.1.68) is a type of amylase, a group of enzymes that break down complex carbohydrates, specifically starch and glycogen, into simpler sugars. Isoamylase is more precisely defined as an enzyme that hydrolyzes (breaks down) alpha-1,6 glucosidic bonds in isomaltose, panose, and dextrins, yielding mainly isomaltose and limit dextrin. It is found in various organisms, including bacteria, fungi, and plants. In humans, isoamylase is involved in the digestion of starch in the small intestine, where it helps convert complex carbohydrates into glucose for energy absorption.
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."
Pancreatic juice is an alkaline fluid secreted by the exocrine component of the pancreas, primarily containing digestive enzymes such as amylase, lipase, and trypsin. These enzymes aid in the breakdown of carbohydrates, fats, and proteins, respectively, in the small intestine during the digestion process. The bicarbonate ions present in pancreatic juice help neutralize the acidic chyme that enters the duodenum from the stomach, creating an optimal environment for enzymatic activity.
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.
I'm happy to help! However, it seems there might be a bit of confusion here. Starch is not typically considered a medical term, but rather a nutritional and biochemical concept. Here's a brief explanation:
Starch is a complex carbohydrate that serves as the primary form of energy storage in plants. It is made up of long chains of glucose molecules and can be found in various foods such as grains, legumes, fruits, and vegetables. Amylase, an enzyme present in our saliva and digestive system, helps break down starch into simpler sugars during the digestion process so that our bodies can absorb them for energy.
I hope this clarifies any confusion! If you have any other questions or need further information on a medical topic, please don't hesitate to ask.
Sincalide is a synthetic hormone that stimulates the contraction of the gallbladder and the release of digestive enzymes from the pancreas. It is used in diagnostic procedures to help diagnose conditions such as gallstones or obstructions of the bile ducts.
Sincalide is a synthetic form of cholecystokinin (CCK), a hormone that is naturally produced in the body and stimulates the contraction of the gallbladder and the release of digestive enzymes from the pancreas. When sincalide is administered, it mimics the effects of CCK and causes the gallbladder to contract and release bile into the small intestine. This can help doctors see if there are any obstructions or abnormalities in the bile ducts or gallbladder.
Sincalide is usually given as an injection, and its effects can be monitored through imaging tests such as ultrasound or CT scans. It is important to note that sincalide should only be used under the supervision of a healthcare professional, as it can cause side effects such as abdominal pain, nausea, and vomiting.
Salivary alpha-amylases are a type of enzyme that are secreted by the salivary glands in humans and other mammals. These enzymes play a crucial role in the digestion of carbohydrates, specifically starches and glycogen, by breaking down these complex molecules into simpler sugars such as maltose, isomaltose, and maltotriose.
Salivary alpha-amylases are part of a larger family of enzymes known as alpha-amylases, which also include pancreatic alpha-amylases that are secreted by the pancreas and play a similar role in digestion. However, salivary alpha-amylases have some unique properties, such as being more resistant to denaturation by heat and acid than pancreatic alpha-amylases.
Salivary alpha-amylases are also used as a biomarker in forensic science for the identification of individuals, as they exhibit variations in their protein structure that can be used to distinguish between different people. Additionally, changes in salivary alpha-amylase levels have been associated with various physiological and psychological states, such as stress, anxiety, and arousal.
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.
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.
Hyperamylasemia is a medical condition characterized by an elevated level of amylase in the blood. Amylase is an enzyme that is primarily produced by the pancreas and salivary glands, and it plays a crucial role in digesting carbohydrates.
Normally, the levels of amylase in the blood are relatively low, but when there is damage to the pancreas or salivary glands, such as in cases of pancreatitis, salivary gland inflammation, or blockage, the levels of amylase can rise significantly. This condition is called hyperamylasemia.
Mild elevations in amylase levels may not cause any symptoms and may be discovered only during routine blood tests. However, more significant elevations can indicate a serious underlying medical condition that requires prompt treatment. Symptoms of hyperamylasemia may include abdominal pain, nausea, vomiting, fever, and rapid heartbeat.
It is important to note that hyperamylasemia can also be caused by non-pancreatic conditions such as macroamylasemia, a benign condition where large amylase-containing protein complexes are formed and circulate in the bloodstream, leading to elevated amylase levels. Therefore, it is essential to perform further diagnostic tests to determine the underlying cause of hyperamylasemia.
The exocrine portion of the pancreas refers to the part that releases digestive enzymes into the duodenum, which is the first section of the small intestine. These enzymes help in the breakdown of proteins, fats, and carbohydrates in food, enabling their absorption and utilization by the body.
The exocrine pancreas is made up of acinar cells that cluster together to form acini (singular: acinus), which are small sac-like structures. When stimulated by hormones such as secretin and cholecystokinin, these acinar cells release digestive enzymes like amylase, lipase, and trypsin into a network of ducts that ultimately merge into the main pancreatic duct. This duct then joins the common bile duct, which carries bile from the liver and gallbladder, before emptying into the duodenum.
It is important to note that the pancreas has both exocrine and endocrine functions. The endocrine portion of the pancreas consists of the islets of Langerhans, which release hormones like insulin and glucagon directly into the bloodstream, regulating blood sugar levels.
Bethanechol compounds are a type of cholinergic agent used in medical treatment. They are parasympathomimetic drugs, which means they mimic the actions of the neurotransmitter acetylcholine at muscarinic receptors. Specifically, bethanechol compounds stimulate the muscarinic receptors in the smooth muscle of the bladder and gastrointestinal tract, increasing tone and promoting contractions.
Bethanechol is primarily used to treat urinary retention and associated symptoms, such as those that can occur after certain types of surgery or with conditions like spinal cord injury or multiple sclerosis. It works by helping the bladder muscle contract, which can promote urination.
It's important to note that bethanechol should be used with caution, as it can have various side effects, including sweating, increased salivation, flushed skin, and gastrointestinal symptoms like nausea, vomiting, or diarrhea. It may also interact with other medications, so it's crucial to discuss any potential risks with a healthcare provider before starting this treatment.
Salivary proteins and peptides refer to the diverse group of molecules that are present in saliva, which is the clear, slightly alkaline fluid produced by the salivary glands in the mouth. These proteins and peptides play a crucial role in maintaining oral health and contributing to various physiological functions.
Some common types of salivary proteins and peptides include:
1. **Mucins**: These are large, heavily glycosylated proteins that give saliva its viscous quality. They help to lubricate the oral cavity, protect the mucosal surfaces, and aid in food bolus formation.
2. **Amylases**: These enzymes break down carbohydrates into simpler sugars, initiating the digestive process even before food reaches the stomach.
3. **Proline-rich proteins (PRPs)**: PRPs contribute to the buffering capacity of saliva and help protect against tooth erosion by forming a protective layer on tooth enamel.
4. **Histatins**: These are small cationic peptides with antimicrobial properties, playing a significant role in maintaining oral microbial homeostasis and preventing dental caries.
5. **Lactoferrin**: An iron-binding protein that exhibits antibacterial, antifungal, and anti-inflammatory activities, contributing to the overall oral health.
6. **Statherin and Cystatins**: These proteins regulate calcium phosphate precipitation, preventing dental calculus formation and maintaining tooth mineral homeostasis.
Salivary proteins and peptides have attracted significant interest in recent years due to their potential diagnostic and therapeutic applications. Alterations in the composition of these molecules can provide valuable insights into various oral and systemic diseases, making them promising biomarkers for disease detection and monitoring.
Secretory rate refers to the amount or volume of a secretion produced by a gland or an organ over a given period of time. It is a measure of the productivity or activity level of the secreting structure. The secretory rate can be quantified for various bodily fluids, such as saliva, sweat, digestive enzymes, hormones, or milk, depending on the context and the specific gland or organ being studied.
In clinical settings, measuring the secretory rate might involve collecting and analyzing samples over a certain duration to estimate the production rate of the substance in question. This information can be helpful in diagnosing conditions related to impaired secretion, monitoring treatment responses, or understanding the physiological adaptations of the body under different circumstances.
Secretin is a hormone that is produced and released by the S cells in the duodenum, which is the first part of the small intestine. It is released in response to the presence of acidic chyme (partially digested food) entering the duodenum from the stomach. Secretin stimulates the pancreas to produce bicarbonate-rich alkaline secretions, which help neutralize the acidity of the chyme and create an optimal environment for enzymatic digestion in the small intestine.
Additionally, secretin also promotes the production of watery fluids from the liver, which aids in the digestion process. Overall, secretin plays a crucial role in maintaining the pH balance and facilitating proper nutrient absorption in the gastrointestinal tract.
Maltose is a disaccharide made up of two glucose molecules joined by an alpha-1,4 glycosidic bond. It is commonly found in malted barley and is created during the germination process when amylase breaks down starches into simpler sugars. Maltose is less sweet than sucrose (table sugar) and is broken down into glucose by the enzyme maltase during digestion.
An acute disease is a medical condition that has a rapid onset, develops quickly, and tends to be short in duration. Acute diseases can range from minor illnesses such as a common cold or flu, to more severe conditions such as pneumonia, meningitis, or a heart attack. These types of diseases often have clear symptoms that are easy to identify, and they may require immediate medical attention or treatment.
Acute diseases are typically caused by an external agent or factor, such as a bacterial or viral infection, a toxin, or an injury. They can also be the result of a sudden worsening of an existing chronic condition. In general, acute diseases are distinct from chronic diseases, which are long-term medical conditions that develop slowly over time and may require ongoing management and treatment.
Examples of acute diseases include:
* Acute bronchitis: a sudden inflammation of the airways in the lungs, often caused by a viral infection.
* Appendicitis: an inflammation of the appendix that can cause severe pain and requires surgical removal.
* Gastroenteritis: an inflammation of the stomach and intestines, often caused by a viral or bacterial infection.
* Migraine headaches: intense headaches that can last for hours or days, and are often accompanied by nausea, vomiting, and sensitivity to light and sound.
* Myocardial infarction (heart attack): a sudden blockage of blood flow to the heart muscle, often caused by a buildup of plaque in the coronary arteries.
* Pneumonia: an infection of the lungs that can cause coughing, chest pain, and difficulty breathing.
* Sinusitis: an inflammation of the sinuses, often caused by a viral or bacterial infection.
It's important to note that while some acute diseases may resolve on their own with rest and supportive care, others may require medical intervention or treatment to prevent complications and promote recovery. If you are experiencing symptoms of an acute disease, it is always best to seek medical attention to ensure proper diagnosis and treatment.
Pancreatic diseases refer to a group of medical conditions that affect the structure and function of the pancreas, a vital organ located in the abdomen. The pancreas has two main functions: an exocrine function, which involves the production of digestive enzymes that help break down food in the small intestine, and an endocrine function, which involves the production of hormones such as insulin and glucagon that regulate blood sugar levels.
Pancreatic diseases can be broadly classified into two categories: inflammatory and non-inflammatory. Inflammatory pancreatic diseases include conditions such as acute pancreatitis, which is characterized by sudden inflammation of the pancreas, and chronic pancreatitis, which is a long-term inflammation that can lead to scarring and loss of function.
Non-inflammatory pancreatic diseases include conditions such as pancreatic cancer, which is a malignant tumor that can arise from the cells of the pancreas, and benign tumors such as cysts or adenomas. Other non-inflammatory conditions include pancreatic insufficiency, which can occur when the pancreas does not produce enough digestive enzymes, and diabetes mellitus, which can result from impaired insulin production or action.
Overall, pancreatic diseases can have serious consequences on a person's health and quality of life, and early diagnosis and treatment are essential for optimal outcomes.
Clinical enzyme tests are laboratory tests that measure the amount or activity of certain enzymes in biological samples, such as blood or bodily fluids. These tests are used to help diagnose and monitor various medical conditions, including organ damage, infection, inflammation, and genetic disorders.
Enzymes are proteins that catalyze chemical reactions in the body. Some enzymes are found primarily within specific organs or tissues, so elevated levels of these enzymes in the blood can indicate damage to those organs or tissues. For example, high levels of creatine kinase (CK) may suggest muscle damage, while increased levels of aspartate aminotransferase (AST) and alanine aminotransferase (ALT) can indicate liver damage.
There are several types of clinical enzyme tests, including:
1. Serum enzyme tests: These measure the level of enzymes in the blood serum, which is the liquid portion of the blood after clotting. Examples include CK, AST, ALT, alkaline phosphatase (ALP), and lactate dehydrogenase (LDH).
2. Urine enzyme tests: These measure the level of enzymes in the urine. An example is N-acetyl-β-D-glucosaminidase (NAG), which can indicate kidney damage.
3. Enzyme immunoassays (EIAs): These use antibodies to detect and quantify specific enzymes or proteins in a sample. They are often used for the diagnosis of infectious diseases, such as HIV or hepatitis.
4. Genetic enzyme tests: These can identify genetic mutations that cause deficiencies in specific enzymes, leading to inherited metabolic disorders like phenylketonuria (PKU) or Gaucher's disease.
It is important to note that the interpretation of clinical enzyme test results should be done by a healthcare professional, taking into account the patient's medical history, symptoms, and other diagnostic tests.
Pancreatic alpha-amylases are a type of enzyme that is produced and secreted by the exocrine cells (acinar cells) of the pancreas. These enzymes play an essential role in digesting carbohydrates, particularly starches and glycogen, which are complex forms of carbohydrates found in various foods like grains, potatoes, and legumes.
Alpha-amylases break down these complex carbohydrates into smaller, simpler sugars, such as maltose, maltotriose, and glucose, allowing for their absorption and utilization by the body. The pancreatic alpha-amylases are released into the duodenum, the first part of the small intestine, along with other digestive enzymes during the process of digestion.
In addition to pancreatic alpha-amylases, salivary glands also produce a form of amylase called salivary alpha-amylase, which initiates the breakdown of starches in the mouth through mastication (chewing). However, the majority of carbohydrate digestion occurs in the small intestine with the help of pancreatic alpha-amylases and other enzymes produced by the intestinal lining.
A trisaccharide is a type of carbohydrate molecule composed of three monosaccharide units joined together by glycosidic bonds. Monosaccharides are simple sugars, such as glucose, fructose, and galactose, which serve as the building blocks of more complex carbohydrates.
In a trisaccharide, two monosaccharides are linked through a glycosidic bond to form a disaccharide, and then another monosaccharide is attached to the disaccharide via another glycosidic bond. The formation of these bonds involves the loss of a water molecule (dehydration synthesis) between the hemiacetal or hemiketal group of one monosaccharide and the hydroxyl group of another.
Examples of trisaccharides include raffinose (glucose + fructose + galactose), maltotriose (glucose + glucose + glucose), and melezitose (glucose + fructose + glucose). Trisaccharides can be found naturally in various foods, such as honey, sugar beets, and some fruits and vegetables. They play a role in energy metabolism, serving as an energy source for the body upon digestion into monosaccharides, which are then absorbed into the bloodstream and transported to cells for energy production or storage.
Carbachol is a cholinergic agonist, which means it stimulates the parasympathetic nervous system by mimicking the action of acetylcholine, a neurotransmitter that is involved in transmitting signals between nerves and muscles. Carbachol binds to both muscarinic and nicotinic receptors, but its effects are more pronounced on muscarinic receptors.
Carbachol is used in medical treatments to produce miosis (pupil constriction), lower intraocular pressure, and stimulate gastrointestinal motility. It can also be used as a diagnostic tool to test for certain conditions such as Hirschsprung's disease.
Like any medication, carbachol can have side effects, including sweating, salivation, nausea, vomiting, diarrhea, bradycardia (slow heart rate), and bronchoconstriction (narrowing of the airways in the lungs). It should be used with caution and under the supervision of a healthcare professional.
Amylase
Β-Amylase
Α-Amylase
Alpha amylase inhibitor
List of amylase-induced fermentations
Arthur W. Thomas
Oligosaccharide 4-alpha-D-glucosyltransferase
Direct linear plot
Michaelis-Menten kinetics
Exoenzyme
Lanser Moor
Pancreatic enzymes (medication)
Mumps
Acute pancreatitis
Reference ranges for blood tests
Plant defensin
Croissant
Glucan 1,4-alpha-maltohydrolase
Beer chemistry
Cervix
Caldimonas taiwanensis
Arthrobacter psychrolactophilus
AMY1C
Red imported fire ant
Pancreatic fistula
Edmond H. Fischer
Glycoside hydrolase family 14
ase
Neurturin
Forensic serology
Amylase - Wikipedia
Microbiology] Zymogram for amylase
Amylase Test | HealthLink BC
Amylase: Reference Range, Interpretation, Collection and Panels
Amylase
1QHP: FIVE-DOMAIN ALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE COMPLEX
Amylase Test: MedlinePlus Medical Test
Assessment of Antioxidative and Alpha-Amylase Potential of Polyherbal Extract
T 1958/11 (Amylase variants/NOVOZYMES) 01-03-2016 | Epo.org
Elevated Amylase and Lipase: Physiology Including Non-pancreatitis related Elevations | SpringerLink
Alpha-Amylase, Granules, 100 g | Carolina Biological Supply
β-Amylase (Barley) | Diagnostic & Research Enzymes | Neogen
Elevated Amylase and Lipase, enlarged bile duct and abd pain - Gastroenterology - MedHelp
Amylase Enzymes | MoreBeer
Pancreatic Amylase | Reagent | Randox Laboratories
Amylase Cajun Dance Party Chords and Lyrics for Guitar
Amylase - Tufts Observer
Amylase (Fluid) - Clinical Biochemistry
alpha-amylase Archives - Ideas Galore
Properties of the Alpha Amylase from Moringa oleifera Seeds
2021 - 5th International Infogest Webinar on Food Digestion: Digestive amylases and starch digestion - Teagasc | Agriculture...
Pancreatic Amylase Test In Baytown | Any Lab Test Now
SciELO - Brazil - Culture conditions for the production of thermostable amylase by Bacillus sp Culture conditions for the...
Recombinant Arabidopsis thaliana Beta-amylase 1, chloroplastic (BAM1) , partial | CSB-YP878501DOA | Cusabio
Do low lipase & amylase levels indicate a health issue?
Amylase Diastase Assignment Help By Online Tutoring Sessions | AssignmentHelp.Net
PuraDyme Amylase Individual Enzyme (180 caps)
Magnitude of Changes in the Activity of Amylases and Cellulase and its Association with the Biochemical Composition during...
Hypothesis that alpha-amylase evokes regulatory mechanisms originating in the pancreas, gut and circulation, which govern...
Beta amylase11
- Different temperatures optimize the activity of alpha or beta amylase, resulting in different mixtures of fermentable and unfermentable sugars. (wikipedia.org)
- In the mash, we are really concerned with two main enzymes: alpha and beta amylase. (morebeer.com)
- It will convert starch to soluble sugars in a temperature range from 145 to 158 °F. Beta amylase is mostly responsible for creating large amounts of fermentable sugar. (morebeer.com)
- It is typically active between131 and 149 °F. As your mash approaches 149 °F, the beta amylase is working at its fastest, but it is also denaturing rapidly. (morebeer.com)
- A lower temperature mash will create more beta amylase, which will create a wort that is more fermentable, but may yield slightly less extract and have less body. (morebeer.com)
- If you are aiming for a mash temperature above 149 and you utilize a single-infusion mash, then you run the risk of denaturing the beta amylase very quickly and diminishing its effects. (morebeer.com)
- If you are planning on mashing at a higher temperature, then you could opt to do a beta amylase rest within the enzyme's optimal temperature range to increase the wort's fermentability before raising the temperature into alpha amylase's optimal temperature range. (morebeer.com)
- The optimal pH for alpha amylase is 5.3-5.7 while the optimal range for beta amylase is 5.1-5.3. (morebeer.com)
- A thicker mash can add some temperature insulation for the beta amylase, while a thinner mash will result in alpha amylase being more prominent. (morebeer.com)
- Amylase is divided in three types : a) Alpha-amylase, b) Beta-amylase, and c) Gamma-amylase. (assignmenthelp.net)
- Amylases (which include both alpha amylase and beta amylase) are the major category of starch degrading enzymes and cellulase is responsible for the cell wall (cellulose) degradation in fruit tissue that results in tissue softening. (omicsonline.org)
Enzymes17
- The pancreas and salivary gland make amylase (alpha amylase) to hydrolyse dietary starch into disaccharides and trisaccharides which are converted by other enzymes to glucose to supply the body with energy. (wikipedia.org)
- While amylases are found naturally in yeast cells, it takes time for the yeast to produce enough of these enzymes to break down significant quantities of starch in the bread. (wikipedia.org)
- Amylases are enzymes that catalyze the hydrolysis of amylopectin, amylose, glycogen, and their hydrolyzed products into simple and easily digestible sugars. (medscape.com)
- Waits another 10 seconds…* For the 3 of you that stayed and decided that you are in for the long haul, we are going to be learning about amylase enzymes and the roles they play in the brewing process. (morebeer.com)
- When it comes to brewing, amylase enzymes play a major role in the mashing process. (morebeer.com)
- There are several different amylase enzymes, including ptyalin, which is an amylase enzyme present in your saliva that begins the digestion process by breaking down some simple starches (this is largely the reason why things like crackers will break down and dissolve in your mouth). (morebeer.com)
- The last way that we can affect these enzyme actions is by adding commercially available, food-grade amylase enzymes directly to the mash. (morebeer.com)
- Adding amylase enzymes to your mash will increase the rates of these reactions by providing more enzymes to break down sugars before total denaturation occurs. (morebeer.com)
- Adding amylase enzymes can be helpful when brewing a beer that utilizes a large percentage of specialty malts that have been kilned at high enough temperature to denature most of the natural amylase enzymes typically found in barley. (morebeer.com)
- Recent discoveries of starch degrading enzymes have led to increased application of amylases in various industrial processes (1). (scielo.br)
- Recent research with thermostable a-amylases has concentrated on the enzymes of thermophiles and extreme thermophiles (2,3,7,8,16,17,20) and little is known about the properties of the enzymes produced by these organisms. (scielo.br)
- Amylase is a type of enzymes which is made-up of proteins, whose activity basically depends on their shapes and structures. (assignmenthelp.net)
- to investigate the activity of two major degrading enzymes - amylases and cellulase during fruit maturation and ripening. (omicsonline.org)
- The blocking group in BPNPG7 prevents hydrolysis of this substrate by exo -acting enzymes such as amyloglucosidase, α-glucosidase, and β-amylase. (megazyme.com)
- Amylase is the name given to glycoside hydrolase enzymes that break down starch into maltose molecules. (wikidoc.org)
- Modern bread making techniques have included amylase enzymes into bread improver thereby making the bread making process faster and more practical for commercial use. (wikidoc.org)
- Amylase, along with other enzymes, is produced by the pancreas to digest carbohydrates. (leadgravy.com)
Serum10
- 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)
- Karsenti D, Bacq Y, Brechot J, Mariotte N, Vol S, Tichet J. Serum amylase and lipase activities in normal pregnancy: a prospective case-control study. (springer.com)
- Prevalence of normal serum amylase levels in patients with acute alcoholic pancreatitis. (springer.com)
- Got a blood test @ Labcorp, Amylase, serum. (healthtap.com)
- Chen CB, McCall NS, Pucci MJ, Leiby B, Dabbish N, Winter JM, Yeo CJ, Lavu H. The Combination of Pancreas Texture and Postoperative Serum Amylase in Predicting Pancreatic Fistula Risk. (jefferson.edu)
Form of amylase found2
- A form of amylase found in bacteria , molds, yeast s, and the seed s of plants that cuts alpha-bonds of large sugar molecules (e.g. starch, glycogen , and related polysaccharide s), removing the successive beta-maltose units from the non-reducing ends of the chains. (biologyonline.com)
- Alpha amylase is the major form of amylase found in humans and other mammals. (upcfoodsearch.com)
Malted barley2
- In traditional beer brewing, malted barley is mixed with hot water to create a "mash", which is held at a given temperature to allow the amylases in the malted grain to convert the barley's starch into sugars. (wikipedia.org)
- Modern breadmaking techniques have included amylases (often in the form of malted barley) into bread improver, thereby making the process faster and more practical for commercial use. (wikipedia.org)
Substrate8
- Because it can act anywhere on the substrate, α-amylase tends to be faster-acting than β-amylase. (wikipedia.org)
- Activation of Bacillus licheniformis α-amylase through a disorder to order transition of the substrate binding site mediated by a calcium-sodium-calcium metal triad. (scialert.net)
- Carbohydrate binding sites in a pancreatic α-amylase-substrate complex derived from x-ray structure analysis at 2.1Ao resolution. (scialert.net)
- Protein engineering in the α-amylase family: Catalytic mechanism substrate specificity and stability. (scialert.net)
- The present thesis concerns studies of two α-amylases: 1) secondary substrate binding sites in barley α-amylase 1 (AMY1), and 2) the involvement of anti-nutrients in in vitro digestion of starch in legumes by porcine pancreatic α-amylase. (dtu.dk)
- Aliquots of diluted extract (containing α-amylase) were incubated with substrate mixture under defined conditions of pH, temperature, and time. (megazyme.com)
- When the substrate is cleaved by endo-acting α-amylase, the nitrophenyl oligosaccharide is immediately and completely hydrolyzed to p -nitrophenol and free glucose by the excess quantities of α-glucosidase present in the substrate mixture. (megazyme.com)
- Gathered data revealed an unusual action pattern of sequential α- amylase treatment at high substrate concentrations. (bvsalud.org)
Lipase14
- In acute pancreatitis , elevated amylase concentrations usually parallel levels of another enzyme called lipase. (labtestsonline.org.uk)
- Either amylase or lipase can be requested in order to help diagnose acute pancreatitis, but amylase is the most frequently used test. (labtestsonline.org.uk)
- Elevated amylase and/or lipase levels greater than three times the upper limit of normal in an appropriate clinical setting are suggestive of pancreatitis. (springer.com)
- Pancreatitis can occur with normal or mild degree of amylase and lipase elevations, and thus, cross-sectional imaging can be helpful. (springer.com)
- Severity of disease does not correlate with the degree of elevations of amylase and/or lipase. (springer.com)
- Frank B, Gottlieb K. Amylase normal, lipase elevated: is it pancreatitis? (springer.com)
- Evaluation of amylase and lipase in the diagnosis of acute pancreatitis. (springer.com)
- Lankisch PG, Burchard-Reckert S, Lehnick D. Underestimation of acute pancreatitis: patients with only a small increase in amylase/lipase levels can also have or develop severe acute pancreatitis. (springer.com)
- I was told I had the flu and then after two weeks they admitted me into the hospital and found out that my amylase and lipase was elevated. (medhelp.org)
- Do low lipase & amylase levels indicate a health issue? (healthtap.com)
- Does low lipase and amylase in healthy individual indicate a health issue? (healthtap.com)
- What do you suggest if my sister has elevated lipase and amylase. (healthtap.com)
- My sister has elevated lipase and amylase. (healthtap.com)
- Lipase has never been elevated but amylase fluctuates. (healthtap.com)
Bacillus5
- The α-amylase form is also found in plants, fungi (ascomycetes and basidiomycetes) and bacteria (Bacillus). (wikipedia.org)
- Purification and properties of β-amylase produced by Bacillus polymyxa . (scialert.net)
- In these days amylase is produced by bacteria called Bacillus amyloliquefaciens P-001. (assignmenthelp.net)
- Hydrolysis of highly concentrated soluble starch (60%, w/w) was performed using sequential α- amylases from Bacillus stearothermophilus (T, 0.2%, w/w) and Bacillus amyloliquefaciens (B, 0.1%, w/w) to identify their possible action patterns. (bvsalud.org)
- Bacillus stearothermophilus α- amylase exhibited more pronounced endo- hydrolysis of amylopectin , whereas the attack of Bacillus amyloliquefaciens α- amylase on the exterior chains was enhanced in amylopectin residues. (bvsalud.org)
Starch into maltose1
- During the ripening of fruit, β-amylase breaks starch into maltose, resulting in the sweet flavor of ripe fruit. (wikipedia.org)
Diastase2
- To submit Amylase (Diastase) assignment click here . (assignmenthelp.net)
- Under the original name of diastase , amylase was the first enzyme to be found and isolated (by Anselme Payen in 1833). (wikidoc.org)
Saliva3
- Amylase is present in the saliva of humans and some other mammals, where it begins the chemical process of digestion. (wikipedia.org)
- Amylase molecule from human saliva. (medscape.com)
- They also provided saliva samples for cortisol and alpha-amylase (AA) prior to and 5, 20 and 40 min post-mTSST. (salimetrics.com)
Pancreatic diseases2
- The blood test for amylase is used to diagnose acute pancreatitis (inflammation of the pancreas) and other pancreatic diseases . (labtestsonline.org.uk)
- Amylase measurements are used primarily for the diagnosis and treatment of pancreatitis (severe inflammation of the pancreas) as well as pancreatic diseases. (randox.com)
Pancreatitis9
- The ratio of amylase urinary clearance to creatinine clearance can be used in the diagnosis of acute and relapsing pancreatitis. (medscape.com)
- The swift rise of amylase at the beginning of a pancreatitis attack, and its fall after about 2 days, helps to pinpoint this diagnosis. (labtestsonline.org.uk)
- In pancreatitis which is a severe inflammation of the pancreas, amylase concentrations are usually very high, often 5-10 times normal. (labtestsonline.org.uk)
- Tests for amylase in blood or urine are mainly used to diagnose problems with your pancreas, including pancreatitis , which is an inflammation of the pancreas. (medlineplus.gov)
- Amylase levels rise quickly at the start of a pancreatitis attack and fall after around 2 days. (randox.com)
- When the pancreas or the salivary glands are damaged, more amylase is released into the blood during an initial or acute attack of pancreatitis. (leadgravy.com)
- An Amylase test may be ordered when a person exhibits symptoms of pancreatitis (an infection of the pancreas). (leadgravy.com)
- With acute pancreatitis (short term or new onset) amylase levels may rise to as high as 4 to 6 times the normal level. (leadgravy.com)
- Low results could indicate damage to the pancreas from long term pancreatitis that prevents the pancreas from producing amylase. (leadgravy.com)
Level of amylase1
- The Amylase Test is a blood test that measures the level of amylase in the blood. (anylabtestnow.com)
Levels of amylase1
- Normally, only low levels of amylase are found in the blood or urine. (healthlinkbc.ca)
High amylase1
- A high amylase result due to macroamylase is not an indicator of disease. (labtestsonline.org.uk)
Salivary amylase4
- 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)
- Human salivary amylase. (wikidoc.org)
Saccharogen amylase2
- saccharogen amylase) is also synthesized by bacteria, fungi, and plants. (wikipedia.org)
- saccharogen amylase) Another form of amylase, β-amylase is also synthesized by bacteria , fungi , and plants . (wikidoc.org)
Extracellular4
- Many microbes also produce amylase to degrade extracellular starches. (wikipedia.org)
- Purification and properties of extracellular amylase from the hyperthermophilic archaeon Thermococcus profundus DT5432. (scialert.net)
- Purification and characterization of extracellular α-amylase produced by Lactobacillus maninotivorans LMG 18010T, an amylolytic lactic acid bacterium. (scialert.net)
- this indicates an endo-type (random cleavage) of extracellular amylase reaction in the bacteria under study. (vuzv.cz)
Hydrolysis2
- An amylase (/ˈæmɪleɪs/) is an enzyme that catalyses the hydrolysis of starch (Latin amylum) into sugars. (wikipedia.org)
- Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units (maltose) at a time. (wikipedia.org)
Germination5
- β-amylase is present in an inactive form prior to germination, whereas α-amylase and proteases appear once germination has begun. (wikipedia.org)
- NIScPR Online Periodical Repository: Amylase induction during seed germination in isoproturon susceptible and resistant biotypes of Phalaris minor Retz. (niscair.res.in)
- The activity of amylase and protease inhibitors in AG 5011 and CD 307 hybrids were determined during germination with controlled and not controlled conditions of temperature and relative humidity and, they were correlated to maize resistance against Sithophilus zeamais. (bvsalud.org)
- Amylase and protease inhibitory activity increased during germination in both hybrids, which ranged respectively from 2.8 to 39.5 UIA/g, and 550.0 to 3633.9 UIP/g. (bvsalud.org)
- amylase) (EC 3.2.1.1) is an endo-amylolytic enzyme that plays an important role in seed germination in wheat. (jscimedcentral.com)
Bacteria2
- Plants and some bacteria also produce amylase. (wikipedia.org)
- The activity and cellular localization of amylases was determined in 9 bacteria identified as strains of Actinomyces israeli, Bacteroides spp. (vuzv.cz)
Thermostable2
- Thermostable pullulanase and α-amylase activity from Clostridium thermosulfurogenes SV9 optimization of culture conditions for enzyme production. (scialert.net)
- A new amylase assay reagent containing p -nitrophenyl α-D-maltoheptaoside (blocked) plus a thermostable α-glucosidase. (megazyme.com)
Maltose3
- By acting at random locations along the starch chain, α-amylase breaks down long-chain saccharides, ultimately yielding either maltotriose and maltose from amylose, or maltose, glucose and "limit dextrin" from amylopectin. (wikipedia.org)
- One Unit of β-amylase activity is defined as the amount of enzyme required to release one µmole of maltose reducing-sugar equivalents per minute from soluble starch (10 mg/mL) in sodium phosphate buffer (200 mM), pH 6.0 at 40°C. (neogen.com)
- Hence the activity of Alfa-amylase was measured in terms of mg maltose released during first five minutes. (who.int)
Breaks starch1
- Supplement In plants, the β-amylase breaks starch into sugar, resulting in the. (biologyonline.com)
Pancreas and salivary1
- Most of the amylase in your body is made by your pancreas and salivary glands. (medlineplus.gov)
Proteins4
- Specific amylase proteins are designated by different Greek letters. (wikipedia.org)
- Increased blood amylase with normal or low urine amylase may indicate decreased kidney function or the presence of macroamylase, when amylase is attached to other proteins and accumulates in blood. (labtestsonline.org.uk)
- These are the proteins and binds with active site of amylase, it is nutritional supplements. (assignmenthelp.net)
- 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)
Cereals5
- Cereal β-amylase: Diversity of the β-amylase isoenzyme status with in cereals. (scialert.net)
- β-amylase in cereals: A study of the maize β-amylase system. (scialert.net)
- In cereals grains and their products, level of alpha amylase is significantly affected by industrial exploitation of these commodity. (assignmenthelp.net)
- In General, the development of methods for measuring α-amylase is pioneered in the clinical chemistry field and then translated to other industries, such as the cereals and fermentation industries. (megazyme.com)
- This article describes many of the commonly used methods for measuring α-amylase in the cereals, food, and fermentation industries and discusses some of the advantages and limitations of each. (megazyme.com)
Digestive3
- Animal tissues do not contain β-amylase, although it may be present in microorganisms contained within the digestive tract. (wikipedia.org)
- One or both types of amylase test may also be used to help diagnose or monitor treatment for other disorders that may affect amylase levels, such as salivary gland disorders and certain digestive conditions. (medlineplus.gov)
- Then we can only discus about Alpha- amylase, which play an important role in digestive and metabolic process. (assignmenthelp.net)
Bacterial3
- Studies on the alpha-amylase production were carried out with a bacterial strain isolated from a soil sample. (scielo.br)
- The analyzed samples were white wheat flour, white wheat flour to which fungal α-amylase had been added, milled malt, and fungal and bacterial enzyme preparations. (megazyme.com)
- Studies were made to characterise soluble Alfa-Amylase (Bacterial). (who.int)
Starches3
- 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)
- Digestion and Interaction of Starches with α-Amylases: I. Mutational analysis of Carbohydrate Binding Sites in barley. (dtu.dk)
- Bacilliary amylase is also used in detergents to dissolve starches from fabrics. (wikidoc.org)
Designated by different Greek letters1
- Although the amylases are designated by different Greek letters, they all act on α-1,4- glycosidic bonds . (wikidoc.org)
Blood and urine2
- But if the pancreas or salivary glands become damaged or blocked, more amylase is usually released into the blood and urine. (healthlinkbc.ca)
- A small amount of amylase in your blood and urine is normal. (medlineplus.gov)
Activity15
- The PHF is screened for the phytochemical screening, and then the antidiabetic activity is determined by alpha-amylase inhibition. (hindawi.com)
- In in vitro study, the result revealed polyherbal formulation in which hot water extract has the topmost inhibitory effect on alpha-amylase activity, ranging from 20.4% to 79.5% with an IC50 value of 48.98 ± 0.31 μ g/ml. (hindawi.com)
- Alpha amylase activity was increased in the presence of MnCl 2 , CoCl 2 , ZnCl 2 and CaCl 2 but decreased with ethylene diamine tetra-acetic acid (EDTA), copper sulphate and silver nitrate. (scialert.net)
- α-amylase activity in Salvadora oleides fruit. (scialert.net)
- Release and activity of bound β-amylase in germinating barley grain. (scialert.net)
- Magnitude of Changes in the Activity of Amylases and Cellulase and its Association with the Biochemical Composition during Maturation and Ripening of Banana (Musa spp. (omicsonline.org)
- Results and discussion: Significant variations in the specific activity of amylases and cellulase were observed between different periods of maturity. (omicsonline.org)
- The activity of amylases was found to be very low (4.8 ± 0.26 Units) during the tender stage, remained low up to 90th days (14.00 ± 0.86 Units) of maturation, but when the fruits starts ripening after 90 days it increased to about 10 folds on the 92nd day (103.40 ± 8.20 Units) and then gradually decreased towards the overripe stage ie. (omicsonline.org)
- The activity of amylase and cellulase had significant correlations with the concentrations of related biochemical constituents such as starch and cellulose. (omicsonline.org)
- When liquid whole egg is pasteurised, the efficiency of the pasteurisation can be checked by measuring the reduction in the alpa-amylase activity. (lovibond.com)
- Measurement of α-amylase activity in white wheat flour, milled malt, and microbial enzyme preparations, using the ceralpha assay: Collaborative study. (megazyme.com)
- This study was conducted to evaluate the method performance of a rapid procedure for the measurement of α-amylase activity in flours and microbial enzyme preparations. (megazyme.com)
- Higher amylase activity is observed in the initial hours of imbibition in the resistant biotype. (niscair.res.in)
- Alfa-amylase showed optimal activity at pH 6.0 Cyanogen bromide was prepared and was used to activate sephadex G200 at pH 11.5. (who.int)
- A sample of immobilized Alfa-amylase (prepared at pH 8.3) was tested thrice in 3 weeks for stability on usage and it retained 85 percent of its original activity. (who.int)
Reagent1
- High purity α-Amylase HR Reagent - 4 vials for the measurement of α-amylase for research, biochemical enzyme assays and in vitro diagnostic analysis. (megazyme.com)
Enzyme present1
- Amylase is an enzyme present in pancreatic fluids within the small intestine. (randox.com)
Assay procedures3
- Powder enzyme form (2000°L) is for use in AACC and ASBC α-amylase assay procedures (see E-BARBP). (neogen.com)
- For use in AACC and ASBC α-amylase assay procedures. (neogen.com)
- Specific activities of amylases and cellulase were analyzed by standard assay procedures. (omicsonline.org)
Urine test5
- For a 24-hour urine test for amylase, be sure to drink enough fluids during the test to prevent dehydration . (healthlinkbc.ca)
- Increases and decreases in amylase levels show up in blood before urine, so an amylase urine test may be done with or after an amylase blood test. (medlineplus.gov)
- Your health care provider may order an amylase blood and/or urine test if you have symptoms of a pancreatic disorder. (medlineplus.gov)
- For an amylase urine test, you will need to give a urine sample for the test. (medlineplus.gov)
- You should not drink alcohol for 24 hours before having an amylase blood or urine test. (medlineplus.gov)
Glycogenase1
- glycogenase) The α-amylases are calcium metalloenzymes , completely unable to function in the absence of calcium. (wikidoc.org)
Sugars2
- α- and β-amylases are important in brewing beer and liquor made from sugars derived from starch. (wikipedia.org)
- Amylases are used in breadmaking and to break down complex sugars, such as starch (found in flour), into simple sugars. (wikipedia.org)
Fungal1
- Fungal α-amylase is a liquid fungal alpha-amylase from Aspergillus oryzae. (thehomebrewbarn.com)
Amylopectin1
- 1,4-α- D -glucan glucohydrolase) In addition to cleaving the last α(1-4)glycosidic linkages at the nonreducing end of amylose and amylopectin , yielding glucose , γ-amylase will cleave α(1-6) glycosidic linkages. (wikidoc.org)
Cereal2
- Measurement of α-Amylase in Cereal, Food and Fermentation Products. (megazyme.com)
- Cereal grain amylase is key to the production of malt. (wikidoc.org)
Macroamylasemia1
- Macroamylasemia, an uncommon and harmless condition in which amylase is bound to a protein in the blood. (healthlinkbc.ca)
Wheat4
- Detection and partial characterization of two antigenetically distinct β-amylase in developing kernel of wheat. (scialert.net)
- amylase in post-harvest wheat grains has a negative effect on wheat yield and end-products quality. (jscimedcentral.com)
- A wide range of studies have been carried out on wheat alpha amylase due to its important biological roles in post-harvest spouting. (jscimedcentral.com)
- The inhalable flour dust samples were further analyzed for alpha-amylase and wheat. (cdc.gov)
Protein2
- Amylase is an enzyme, or special protein, that helps you digest carbohydrates . (medlineplus.gov)
- The amounts of protein in the immobilized Alfa-amylase prepared at pH 8.3 and 7.0 were estimated by, Kjeldhal method, by the tryptophan content and from the difference in the amount of protein present in the original solution and that in the washings. (who.int)
Soluble4
- Alpha amylase is responsible for breaking down large, complex, insoluble starch molecules into smaller, soluble molecules. (morebeer.com)
- 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-amylase respectively. (who.int)
- amylases from B. stearothermophilus and B. amyloliquefaciens on highly concentrated soluble starch. (bvsalud.org)
- Analysis of the action pattern of sequential α-amylases from B. stearothermophilus and B. amyloliquefaciens on highly concentrated soluble starch. (bvsalud.org)
Yeast2
- The addition of calcium (10 mM) or peptone (1%) and yeast extract (0.5%) to the mineral medium shortened the lag period and improved the growth and alpha-amylase synthesis. (scielo.br)
- The level of alpha amylase in bread making must be sufficient to produce saccharides, which is used by yeast. (assignmenthelp.net)
Molecule1
- An image depicting an amylase molecule can be seen below. (medscape.com)
Alpha10
- Alpha amylase is of salivary or pancreatic origin and referred to as S-type or P-type amylase, respectively. (medscape.com)
- Crude alpha amylase preparation from Moringa oleifera seeds was used to hydrolyze starch. (scialert.net)
- at 90°C. The stability of alpha amylase was increased in the presence of CoCl 2 . (scialert.net)
- The addition of glucose to the culture diminished greatly the synthesis of alpha-amylase, demonstrating that a classical glucose effect is operative in this organism. (scielo.br)
- The addition of glucose to the culture diminished greatly the synthesis of alpha-amylase. (scielo.br)
- The level of alpha-amylase in brewing industries is a key quality parameters. (assignmenthelp.net)
- They are discussed in much more detail at alpha-Amylase . (wikidoc.org)
- An inhibitor of alpha-amylase called phaseolamin has been tested as a potential diet aid. (wikidoc.org)
- What is Alpha Amylase? (upcfoodsearch.com)
- Koh D, Ng V, Naing L. Alpha amylase as a salivary biomarker of acute stress of venepuncture from periodic medical examinations. (medscape.com)