Disaccharidases are a group of enzymes, including maltase, sucrase, lactase, and trehalase, found primarily in the brush border of the small intestine, responsible for breaking down complex disaccharides into simpler monosaccharides for absorption.
'Sucrase' is an intestinal brush-border enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose in the digestive process.
Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II.
Enzymes that hydrolyze O-glucosyl-compounds. (Enzyme Nomenclature, 1992) EC 3.2.1.-.
The middle portion of the SMALL INTESTINE, between DUODENUM and ILEUM. It represents about 2/5 of the remaining portion of the small intestine below duodenum.
The portion of the GASTROINTESTINAL TRACT between the PYLORUS of the STOMACH and the ILEOCECAL VALVE of the LARGE INTESTINE. It is divisible into three portions: the DUODENUM, the JEJUNUM, and the ILEUM.
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)
A disaccharide of GLUCOSE and GALACTOSE in human and cow milk. It is used in pharmacy for tablets, in medicine as a nutrient, and in industry.
Glycoside Hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds, resulting in the breakdown of complex carbohydrates and oligosaccharides into simpler sugars.
Lining of the INTESTINES, consisting of an inner EPITHELIUM, a middle LAMINA PROPRIA, and an outer MUSCULARIS MUCOSAE. In the SMALL INTESTINE, the mucosa is characterized by a series of folds and abundance of absorptive cells (ENTEROCYTES) with MICROVILLI.
A family of galactoside hydrolases that hydrolyze compounds with an O-galactosyl linkage. EC 3.2.1.-.
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.
Oligosaccharides containing two monosaccharide units linked by a glycosidic bond.
Minute projections of cell membranes which greatly increase the surface area of the cell.
A nonreducing disaccharide composed of GLUCOSE and FRUCTOSE linked via their anomeric carbons. It is obtained commercially from SUGARCANE, sugar beet (BETA VULGARIS), and other plants and used extensively as a food and a sweetener.
A group of enzymes that catalyzes the hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-galactosides. Deficiency of beta-Galactosidase A1 may cause GANGLIOSIDOSIS, GM1.
An infection of the SMALL INTESTINE caused by the flagellated protozoan GIARDIA LAMBLIA. It is spread via contaminated food and water and by direct person-to-person contact.
A species of parasitic EUKARYOTES that attaches itself to the intestinal mucosa and feeds on mucous secretions. The organism is roughly pear-shaped and motility is somewhat erratic, with a slow oscillation about the long axis.
A genus of flagellate intestinal EUKARYOTES parasitic in various vertebrates, including humans. Characteristics include the presence of four pairs of flagella arising from a complicated system of axonemes and cysts that are ellipsoidal to ovoidal in shape.
Infections of the INTESTINES with PARASITES, commonly involving PARASITIC WORMS. Infections with roundworms (NEMATODE INFECTIONS) and tapeworms (CESTODE INFECTIONS) are also known as HELMINTHIASIS.
Infections with unicellular organisms formerly members of the subkingdom Protozoa.
Excrement from the INTESTINES, containing unabsorbed solids, waste products, secretions, and BACTERIA of the DIGESTIVE SYSTEM.
Invertebrate organisms that live on or in another organism (the host), and benefit at the expense of the other. Traditionally excluded from definition of parasites are pathogenic BACTERIA; FUNGI; VIRUSES; and PLANTS; though they may live parasitically.

Uptake of iodinated human kidney alpha-D-mannosidase by rat liver- Association with membrane elements and stability in vivo and in vitro. (1/153)

1. Human kidney alpha-D-mannosidase (form A) was labelled with 125I to a specific radio-activity of approx. 2250muCi/mg of protein, essentially without loss of enzymic activity. The enzymic activity and radioactivity of the iodinated material also co-migrated in gel filtration and gel electrophoresis. 2. The binding of 125I-labelled mannosidase in vitro to particulate material in liver and kidney homogenates was of the other of 2 pg/mg of particulate material in liver and kidney homogenates was of the order of 2pg/mg of particulate protein withing 16h at 37 degrees C, and essentially zero in intervals of up to 60 min. The degradation in vitro of labelled exogenous mannosidase was of the order of 10-20pg/ 16th per mg of protein in postnuclear supernatant, and it was saturated entirely within 1h at 37 degrees C. 3. The binding of labelled mannosidase in vivo to particulate elements of liver homogenates 60 min after intravenous injection was at least 10 times higher in terms of specific radioactivity than the highest value attainable in vitro. Virtually all exogenous enzyme bound to liver particulate material could be recovered in macromolecular form after disruption of membranes by detergents. 4. The radioactive enzyme bound to liver particulate material could be detached almost completely by shearing, repeated freezing and thawing, and exposure to strong detergents under conditions that do not eliminate rough-endoplasmic-membrane structure. It could bot be released, however, by high salt concentration (0.5M-KC1) or by exposure to weak detergents such as Tween 80. The particle-bound enzyme should thus be associated with plasma membranes and lysosome-like elements. 5. Of the rat tissues studied, only liver could approach, within 60 min after the injection, the concentration of exogenous mannosidase found in the blood serum. The activity per g tissue weight fell progressively from liver (60% of serum value) to kidney (16% of serum value), lung (8% of serum vlaue), spleen (6% of serum value) and brain (0.9% of serum value). Most of the radioactive enzyme found in tissues other than liver appeared to be present in a free form, whereas in liver more than 50% of the labelled enzyme was associated with membrane elements.  (+info)

The structural gene for alpha-mannosidase-1 in Dictyostellium discoideum. (2/153)

We have isolated 4 independent mutations affecting alpha-mannosidase-1, a developmentally regulated activity in Dictyrostelium discoideum. Three of these result in a thermolabile alpha-mannosidase-1 activity. One mutation also affects the substrate affinity (Km) of the activity. In diploids these mutations show a gene dosage effect and are all alleles. The structural gene for alpha-mannosidase-1, as defined by these mutations, defines a new linkage group, linkage group VI. alpha-mammosidase 1 is probably a homopolymer with subunits of 54,000 daltons. We have also mapped two temperature-sensitive-for-growth mutations onto two previously defined linkage groups.  (+info)

Saccharomyces boulardii upgrades cellular adaptation after proximal enterectomy in rats. (3/153)

BACKGROUND: Saccharomyces boulardii is a non-pathogenic yeast which exerts trophic effects on human and rat small intestinal mucosa. AIMS: To examine the effects of S boulardii on ileal adaptation after proximal enterectomy in rats. METHODS: Wistar rats, aged eight weeks, underwent 60% proximal resection or transection and received by orogastric intubation either 1 mg/g body wt per day lyophilised S boulardii or the vehicle for seven days. The effects on ileal mucosal adaptation were assessed eight days after surgery. RESULTS: Compared with transection, resection resulted in mucosal hyperplasia with significant decreases in the specific and total activities of sucrase, lactase, and maltase. Treatment of resected animals with S boulardii had no effect on mucosal hyperplasia but did upgrade disaccharidase activities to the levels of the transected group. Enzyme stimulation by S boulardii was associated with significant increases in diamine oxidase activity and mucosal polyamine concentrations. Likewise, sodium dependent D-glucose uptake by brush border membrane vesicles, measured as a function of time and glucose concentration in the incubation medium, was significantly (p<0.05) increased by 81% and three times respectively in the resected group treated with S boulardii. In agreement with this, expression of the sodium/glucose cotransporter-1 in brush border membranes of resected rats treated with S boulardii was enhanced twofold compared with resected controls. CONCLUSION: Oral administration of S boulardii soon after proximal enterectomy improves functional adaptation of the remnant ileum.  (+info)

Physiological roles of gammadelta T-cell receptor intraepithelial lymphocytes in cytoproliferation and differentiation of mouse intestinal epithelial cells. (4/153)

In this study we aimed to elucidate the physiological role of gammadelta intraepithelial lymphocytes (IEL) in the mouse intestine. For this purpose, we used T-cell receptor (TCR) Vgamma4/Vdelta5 transgenic mice (KN 6 Tg: BALB/c background, H-2d), and compared the immunological and physiological characteristics of the intestinal tracts of KN 6 Tg and non-transgenic (non-Tg) littermates. In KN 6 Tg littermates, 95% of small intestinal (SI) and large intestinal (LI) IEL expressed gammadelta TCR, and their TCR was replaced by Tg gammadelta TCR. In these mice, class II major histocompatibility complex (MHC) expression was up-regulated in the SI epithelium, compared with the non-Tg littermates, under specific pathogen-free (SPF) conditions. Competitive reverse transcription-polymerase chain reaction (RT-PCR) analysis showed that the mRNAs of the I-Ealpha chain on the SI epithelial cells was higher in KN 6 Tg than in non-Tg littermates. However, in the LI, class II MHC molecules were not expressed in either KN 6 Tg or non-Tg littermates. The epithelial cell mitotic index in the SI, but not in the LI, was higher in KN 6 Tg than in non-Tg littermates under SPF conditions. However, differentiation markers for SI epithelial cells, such as alkaline phosphatase and disaccharidase (lactase, maltase and sucrase) activities, were similar in KN 6 Tg and non-Tg littermates. MHC class II molecule expression on the SI epithelium was absent in germ-free (GF) Tg mice, but was induced under SPF conditions, coinciding with the increase of interferon-gamma (IFN-gamma) mRNA in gammadelta TCR SI-IEL. These findings suggest that gammadelta TCR IEL regulate epithelial cell regeneration and class II MHC expression, but not cell differentiation in the SI. However, these functions were not observed in the gammadelta TCR IEL in the LI. In addition, the activation step in the gammadelta TCR SI-IEL is dependent on the presence of gut microflora.  (+info)

Bifidobacterium animalis protects intestine from damage induced by zinc deficiency in rats. (5/153)

We investigated the potential beneficial effects of Bifidobacterium animalis on intestinal damage using zinc-deficient (ZD) rats as a model for intestinal alterations. The ZD rats were fed diets containing 1 mg Zn/kg for 20 (ZD(20)) or 40 (ZD(40)) d to induce damage that differed in severity. Subgroups of these rats, the ZD(20) + B and ZD(40) + B groups, received a suspension of B. animalis (3.5 x 10(8) colony forming units) daily for the last 10 d. Another subgroup, the ZD(40) + B + 7 d group, was fed the ZD diet for 7 d after the B. animalis treatment period. Zinc deficiency induced ulcerations, edema, inflammatory cell infiltration and dilatation of blood vessels in duodenum, jejunum and ileum, with increasing severity between 20 and 40 d of zinc deficiency. The mucosa of the ZD(20) + B group was well preserved, and most of the morphologic alterations induced by zinc deficiency were normalized in the ZD(40) + B group. The high fecal concentrations of B. animalis in the ZD(40) + B and ZD(40) + B + 7 d groups indicate that these bifidobacteria survived passage through the gastrointestinal tract and proliferated. Electron microscopy confirmed the elevated numbers of bifidobacteria in cecum. Treatment with B. animalis resulted in greater epithelial cell proliferation and disaccharidase activities in the ZD(40) + B group compared with the ZD(40) group. These findings indicate that B. animalis can protect the intestine from alterations induced by zinc deficiency, suggesting that this bacterium may play a role in intestinal mucosal defense.  (+info)

Acetic acid suppresses the increase in disaccharidase activity that occurs during culture of caco-2 cells. (6/153)

To understand how blood glucose level is lowered by oral administration of vinegar, we examined effects of acetic acid on glucose transport and disaccharidase activity in Caco-2 cells. Cells were cultured for 15 d in a medium containing 5 mmol/L of acetic acid. This chronic treatment did not affect cell growth or viability, and furthermore, apoptotic cell death was not observed. Glucose transport, evaluated with a nonmetabolizable substrate, 3-O-methyl glucose, also was not affected. However, the increase of sucrase activity observed in control cells (no acetic acid) was significantly suppressed by acetic acid (P < 0.01). Acetic acid suppressed sucrase activity in concentration- and time-dependent manners. Similar treatments (5 mmol/L and 15 d) with other organic acids such as citric, succinic, L-maric, L-lactic, L-tartaric and itaconic acids, did not suppress the increase in sucrase activity. Acetic acid treatment (5 mmol/L and 15 d) significantly decreased the activities of disaccharidases (sucrase, maltase, trehalase and lactase) and angiotensin-I-converting enzyme, whereas the activities of other hydrolases (alkaline phosphatase, aminopeptidase-N, dipeptidylpeptidase-IV and gamma-glutamyltranspeptidase) were not affected. To understand mechanisms underlying the suppression of disaccharidase activity by acetic acid, Northern and Western analyses of the sucrase-isomaltase complex were performed. Acetic acid did not affect the de novo synthesis of this complex at either the transcriptional or translational levels. The antihyperglycemic effect of acetic acid may be partially due to the suppression of disaccharidase activity. This suppression seems to occur during the post-translational processing.  (+info)

Relation of the disaccharidases in the small intestine of the rat to the degree of experimentally induced iron-deficiency anemia. (7/153)

Hypolactasia associated with severe iron-deficiency anemia has been reported in several studies. The objective of the present study was to determine whether hypolactasia is associated with the degree and duration of iron-deficiency anemia. Newly weaned male Wistar rats were divided into a control group receiving a diet supplemented with iron (C) and an experimental group (E) receiving a diet not supplemented with iron (iron-deficiency diet). The animals were studied on the 3rd, 5th, 7th, 14th, 21st, 28th and 35th days of the experiment, when overall and iron nutritional status and disaccharidase activity in the small intestine were determined by the Dahlqvist method. A reduction in weight occurred in the anemic animals starting on the 5th day of the study. Anemia was present in the experimental animals, with a progressive worsening up to the 14th day (hemoglobin: C = 13.27 and E = 5.37) and stabilizing thereafter. Saccharase and maltase activities did not differ significantly between groups, whereas lactase showed a significant reduction in total (TA) and specific activity (SA) in the anemic animals starting on the 21st day of the study. Median lactase TA for the C and E groups was 2.27 and 1.25 U on the 21st day, 2.87 and 1. 88 U on the 28th day, and 4.20 and 1.59 U on the 35th day, respectively. Median lactase SA was 0.31 and 0.20 U/g wet weight on the 21st day, 0.39 and 0.24 U/g wet weight on the 28th day, and 0.42 and 0.23 U/g wet weight on the 35th day, respectively. These findings suggest a relationship between the enzymatic alterations observed and both the degree and duration of the anemic process. Analysis of other studies on intestinal disaccharidases in anemia suggests that the mechanism of these changes may be functional, i.e., that the enterocytes may suffer a reduction in their ability to synthesize these enzymes.  (+info)

Determinants of translocation and folding of TreF, a trehalase of Escherichia coli. (8/153)

One isoform of trehalase, TreF, is present in the cytoplasm and a second, TreA, in the periplasm. To study the questions of why one enzyme is exported efficiently and the other is not and whether these proteins can fold in their nonnative cellular compartment, we fused the signal sequence of periplasmic TreA to cytoplasmic TreF. Even though this TreF construct was exported efficiently to the periplasm, it was not active. It was insoluble and degraded by the periplasmic serine protease DegP. To determine why TreF was misfolded in the periplasm, we isolated and characterized Tre(+) revertants of periplasmic TreF. To further characterize periplasmic TreF, we used a genetic selection to isolate functional TreA-TreF hybrids, which were analyzed with respect to solubility and function. These data suggested that a domain located between residues 255 and 350 of TreF is sufficient to cause folding problems in the periplasm. In contrast to TreF, periplasmic TreA could fold into the active conformation in its nonnative cellular compartment, the cytoplasm, after removal of its signal sequence.  (+info)

Disaccharidases are a group of enzymes found in the brush border of the small intestine. They play an essential role in digesting complex carbohydrates into simpler sugars, which can then be absorbed into the bloodstream. The three main disaccharidases are:

1. Maltase-glucoamylase: This enzyme breaks down maltose (a disaccharide formed from two glucose molecules) and maltotriose (a trisaccharide formed from three glucose molecules) into individual glucose units.
2. Sucrase: This enzyme is responsible for breaking down sucrose (table sugar, a disaccharide composed of one glucose and one fructose molecule) into its component monosaccharides, glucose and fructose.
3. Lactase: This enzyme breaks down lactose (a disaccharide formed from one glucose and one galactose molecule) into its component monosaccharides, glucose and galactose.

Deficiencies in these disaccharidases can lead to various digestive disorders, such as lactose intolerance (due to lactase deficiency), sucrase-isomaltase deficiency, or congenital sucrase-isomaltase deficiency (CSID). These conditions can cause symptoms like bloating, diarrhea, and abdominal cramps after consuming foods containing the specific disaccharide.

Sucrase is a digestive enzyme that is produced by the cells lining the small intestine. Its primary function is to break down sucrose, also known as table sugar or cane sugar, into its component monosaccharides: glucose and fructose. This process allows for the absorption of these simple sugars into the bloodstream, where they can be used as energy sources by the body's cells.

Sucrase is often deficient in people with certain genetic disorders, such as congenital sucrase-isomaltase deficiency (CSID), which leads to an impaired ability to digest sucrose and results in gastrointestinal symptoms like bloating, diarrhea, and abdominal pain after consuming sugary foods or beverages. In these cases, a sucralose-based diet may be recommended to alleviate the symptoms.

Alpha-glucosidases are a group of enzymes that break down complex carbohydrates into simpler sugars, such as glucose, by hydrolyzing the alpha-1,4 and alpha-1,6 glycosidic bonds in oligosaccharides, disaccharides, and polysaccharides. These enzymes are located on the brush border of the small intestine and play a crucial role in carbohydrate digestion and absorption.

Inhibitors of alpha-glucosidases, such as acarbose and miglitol, are used in the treatment of type 2 diabetes to slow down the digestion and absorption of carbohydrates, which helps to reduce postprandial glucose levels and improve glycemic control.

Glucosidases are a group of enzymes that catalyze the hydrolysis of glycosidic bonds, specifically at the non-reducing end of an oligo- or poly saccharide, releasing a single sugar molecule, such as glucose. They play important roles in various biological processes, including digestion of carbohydrates and the breakdown of complex glycans in glycoproteins and glycolipids.

In the context of digestion, glucosidases are produced by the pancreas and intestinal brush border cells to help break down dietary polysaccharides (e.g., starch) into monosaccharides (glucose), which can then be absorbed by the body for energy production or storage.

There are several types of glucosidases, including:

1. α-Glucosidase: This enzyme is responsible for cleaving α-(1→4) and α-(1→6) glycosidic bonds in oligosaccharides and disaccharides, such as maltose, maltotriose, and isomaltose.
2. β-Glucosidase: This enzyme hydrolyzes β-(1→4) glycosidic bonds in cellobiose and other oligosaccharides derived from plant cell walls.
3. Lactase (β-Galactosidase): Although not a glucosidase itself, lactase is often included in this group because it hydrolyzes the β-(1→4) glycosidic bond between glucose and galactose in lactose, yielding free glucose and galactose.

Deficiencies or inhibition of these enzymes can lead to various medical conditions, such as congenital sucrase-isomaltase deficiency (an α-glucosidase deficiency), lactose intolerance (a lactase deficiency), and Gaucher's disease (a β-glucocerebrosidase deficiency).

The jejunum is the middle section of the small intestine, located between the duodenum and the ileum. It is responsible for the majority of nutrient absorption that occurs in the small intestine, particularly carbohydrates, proteins, and some fats. The jejunum is characterized by its smooth muscle structure, which allows it to contract and mix food with digestive enzymes and absorb nutrients through its extensive network of finger-like projections called villi.

The jejunum is also lined with microvilli, which further increase the surface area available for absorption. Additionally, the jejunum contains numerous lymphatic vessels called lacteals, which help to absorb fats and fat-soluble vitamins into the bloodstream. Overall, the jejunum plays a critical role in the digestion and absorption of nutrients from food.

The small intestine is the portion of the gastrointestinal tract that extends from the pylorus of the stomach to the beginning of the large intestine (cecum). It plays a crucial role in the digestion and absorption of nutrients from food. The small intestine is divided into three parts: the duodenum, jejunum, and ileum.

1. Duodenum: This is the shortest and widest part of the small intestine, approximately 10 inches long. It receives chyme (partially digested food) from the stomach and begins the process of further digestion with the help of various enzymes and bile from the liver and pancreas.
2. Jejunum: The jejunum is the middle section, which measures about 8 feet in length. It has a large surface area due to the presence of circular folds (plicae circulares), finger-like projections called villi, and microvilli on the surface of the absorptive cells (enterocytes). These structures increase the intestinal surface area for efficient absorption of nutrients, electrolytes, and water.
3. Ileum: The ileum is the longest and final section of the small intestine, spanning about 12 feet. It continues the absorption process, mainly of vitamin B12, bile salts, and any remaining nutrients. At the end of the ileum, there is a valve called the ileocecal valve that prevents backflow of contents from the large intestine into the small intestine.

The primary function of the small intestine is to absorb the majority of nutrients, electrolytes, and water from ingested food. The mucosal lining of the small intestine contains numerous goblet cells that secrete mucus, which protects the epithelial surface and facilitates the movement of chyme through peristalsis. Additionally, the small intestine hosts a diverse community of microbiota, which contributes to various physiological functions, including digestion, immunity, and protection against pathogens.

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.

Lactose is a disaccharide, a type of sugar, that is naturally found in milk and dairy products. It is made up of two simple sugars, glucose and galactose, linked together. In order for the body to absorb and use lactose, it must be broken down into these simpler sugars by an enzyme called lactase, which is produced in the lining of the small intestine.

People who have a deficiency of lactase are unable to fully digest lactose, leading to symptoms such as bloating, diarrhea, and abdominal cramps, a condition known as lactose intolerance.

Glycoside hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds found in various substrates such as polysaccharides, oligosaccharides, and glycoproteins. These enzymes break down complex carbohydrates into simpler sugars by cleaving the glycosidic linkages that connect monosaccharide units.

Glycoside hydrolases are classified based on their mechanism of action and the type of glycosidic bond they hydrolyze. The classification system is maintained by the International Union of Biochemistry and Molecular Biology (IUBMB). Each enzyme in this class is assigned a unique Enzyme Commission (EC) number, which reflects its specificity towards the substrate and the type of reaction it catalyzes.

These enzymes have various applications in different industries, including food processing, biofuel production, pulp and paper manufacturing, and biomedical research. In medicine, glycoside hydrolases are used to diagnose and monitor certain medical conditions, such as carbohydrate-deficient glycoprotein syndrome, a rare inherited disorder affecting the structure of glycoproteins.

The intestinal mucosa is the innermost layer of the intestines, which comes into direct contact with digested food and microbes. It is a specialized epithelial tissue that plays crucial roles in nutrient absorption, barrier function, and immune defense. The intestinal mucosa is composed of several cell types, including absorptive enterocytes, mucus-secreting goblet cells, hormone-producing enteroendocrine cells, and immune cells such as lymphocytes and macrophages.

The surface of the intestinal mucosa is covered by a single layer of epithelial cells, which are joined together by tight junctions to form a protective barrier against harmful substances and microorganisms. This barrier also allows for the selective absorption of nutrients into the bloodstream. The intestinal mucosa also contains numerous lymphoid follicles, known as Peyer's patches, which are involved in immune surveillance and defense against pathogens.

In addition to its role in absorption and immunity, the intestinal mucosa is also capable of producing hormones that regulate digestion and metabolism. Dysfunction of the intestinal mucosa can lead to various gastrointestinal disorders, such as inflammatory bowel disease, celiac disease, and food allergies.

Galactosidases are a group of enzymes that catalyze the hydrolysis of galactose-containing sugars, specifically at the beta-glycosidic bond. There are several types of galactosidases, including:

1. Beta-galactosidase: This is the most well-known type of galactosidase and it catalyzes the hydrolysis of lactose into glucose and galactose. It has important roles in various biological processes, such as lactose metabolism in animals and cell wall biosynthesis in plants.
2. Alpha-galactosidase: This enzyme catalyzes the hydrolysis of alpha-galactosides, which are found in certain plant-derived foods like legumes. A deficiency in this enzyme can lead to a genetic disorder called Fabry disease.
3. N-acetyl-beta-glucosaminidase: This enzyme is also known as hexosaminidase and it catalyzes the hydrolysis of N-acetyl-beta-D-glucosamine residues from glycoproteins, glycolipids, and other complex carbohydrates.

Galactosidases are widely used in various industrial applications, such as food processing, biotechnology, and biofuel production. They also have potential therapeutic uses, such as in the treatment of lysosomal storage disorders like Fabry disease.

Alkaline phosphatase (ALP) is an enzyme found in various body tissues, including the liver, bile ducts, digestive system, bones, and kidneys. It plays a role in breaking down proteins and minerals, such as phosphate, in the body.

The medical definition of alkaline phosphatase refers to its function as a hydrolase enzyme that removes phosphate groups from molecules at an alkaline pH level. In clinical settings, ALP is often measured through blood tests as a biomarker for various health conditions.

Elevated levels of ALP in the blood may indicate liver or bone diseases, such as hepatitis, cirrhosis, bone fractures, or cancer. Therefore, physicians may order an alkaline phosphatase test to help diagnose and monitor these conditions. However, it is essential to interpret ALP results in conjunction with other diagnostic tests and clinical findings for accurate diagnosis and treatment.

Disaccharides are a type of carbohydrate that is made up of two monosaccharide units bonded together. Monosaccharides are simple sugars, such as glucose, fructose, or galactose. When two monosaccharides are joined together through a condensation reaction, they form a disaccharide.

The most common disaccharides include:

* Sucrose (table sugar), which is composed of one glucose molecule and one fructose molecule.
* Lactose (milk sugar), which is composed of one glucose molecule and one galactose molecule.
* Maltose (malt sugar), which is composed of two glucose molecules.

Disaccharides are broken down into their component monosaccharides during digestion by enzymes called disaccharidases, which are located in the brush border of the small intestine. These enzymes catalyze the hydrolysis of the glycosidic bond that links the two monosaccharides together, releasing them to be absorbed into the bloodstream and used for energy.

Disorders of disaccharide digestion and absorption can lead to various symptoms, such as bloating, diarrhea, and abdominal pain. For example, lactose intolerance is a common condition in which individuals lack sufficient levels of the enzyme lactase, leading to an inability to properly digest lactose and resulting in gastrointestinal symptoms.

Microvilli are small, finger-like projections that line the apical surface (the side facing the lumen) of many types of cells, including epithelial and absorptive cells. They serve to increase the surface area of the cell membrane, which in turn enhances the cell's ability to absorb nutrients, transport ions, and secrete molecules.

Microvilli are typically found in high density and are arranged in a brush-like border called the "brush border." They contain a core of actin filaments that provide structural support and allow for their movement and flexibility. The membrane surrounding microvilli contains various transporters, channels, and enzymes that facilitate specific functions related to absorption and secretion.

In summary, microvilli are specialized structures on the surface of cells that enhance their ability to interact with their environment by increasing the surface area for transport and secretory processes.

Sucrose is a type of simple sugar, also known as a carbohydrate. It is a disaccharide, which means that it is made up of two monosaccharides: glucose and fructose. Sucrose occurs naturally in many fruits and vegetables and is often extracted and refined for use as a sweetener in food and beverages.

The chemical formula for sucrose is C12H22O11, and it has a molecular weight of 342.3 g/mol. In its pure form, sucrose is a white, odorless, crystalline solid that is highly soluble in water. It is commonly used as a reference compound for determining the sweetness of other substances, with a standard sucrose solution having a sweetness value of 1.0.

Sucrose is absorbed by the body through the small intestine and metabolized into glucose and fructose, which are then used for energy or stored as glycogen in the liver and muscles. While moderate consumption of sucrose is generally considered safe, excessive intake can contribute to weight gain, tooth decay, and other health problems.

Beta-galactosidase is an enzyme that catalyzes the hydrolysis of beta-galactosides into monosaccharides. It is found in various organisms, including bacteria, yeast, and mammals. In humans, it plays a role in the breakdown and absorption of certain complex carbohydrates, such as lactose, in the small intestine. Deficiency of this enzyme in humans can lead to a disorder called lactose intolerance. In scientific research, beta-galactosidase is often used as a marker for gene expression and protein localization studies.

Giardiasis is a digestive infection caused by the microscopic parasite Giardia intestinalis, also known as Giardia lamblia or Giardia duodenalis. The parasite is found worldwide, especially in areas with poor sanitation and unsafe water.

The infection typically occurs after ingesting contaminated water, food, or surfaces that have been exposed to fecal matter containing the cyst form of the parasite. Once inside the body, the cysts transform into trophozoites, which attach to the lining of the small intestine and cause symptoms such as diarrhea, stomach cramps, nausea, dehydration, and greasy stools that may float due to excess fat.

In some cases, giardiasis can lead to lactose intolerance and malabsorption of nutrients, resulting in weight loss and vitamin deficiencies. The infection is usually diagnosed through a stool sample test and treated with antibiotics such as metronidazole or tinidazole. Preventive measures include practicing good hygiene, avoiding contaminated water and food, and washing hands regularly.

"Giardia lamblia," also known as "Giardia duodenalis" or "Giardia intestinalis," is a species of microscopic parasitic protozoan that colonizes and reproduces in the small intestine of various vertebrates, including humans. It is the most common cause of human giardiasis, a diarrheal disease. The trophozoite (feeding form) of Giardia lamblia has a distinctive tear-drop shape and possesses flagella for locomotion. It attaches to the intestinal epithelium, disrupting the normal function of the small intestine and leading to various gastrointestinal symptoms such as diarrhea, stomach cramps, nausea, and dehydration. Giardia lamblia is typically transmitted through the fecal-oral route, often via contaminated food or water.

Giardia is a genus of microscopic parasitic flagellates that cause giardiasis, a type of diarrheal disease. The most common species to infect humans is Giardia intestinalis (also known as Giardia lamblia or Giardia duodenalis). These microscopic parasites are found worldwide, particularly in areas with poor sanitation and unsafe water.

Giardia exists in two forms: the trophozoite, which is the actively feeding form that multiplies in the small intestine, and the cyst, which is the infective stage that is passed in feces and can survive outside the body for long periods under appropriate conditions. Infection occurs when a person ingests contaminated water or food, or comes into direct contact with an infected person's feces.

Once inside the body, the cysts transform into trophozoites, which attach to the lining of the small intestine and disrupt the normal function of the digestive system, leading to symptoms such as diarrhea, stomach cramps, nausea, dehydration, and weight loss. In some cases, giardiasis can cause long-term health problems, particularly in children, including malnutrition and developmental delays.

Preventing the spread of Giardia involves maintaining good hygiene practices, such as washing hands thoroughly after using the toilet or changing diapers, avoiding contaminated water sources, and practicing safe food handling and preparation. In cases where infection occurs, medication is usually effective in treating the illness.

Parasitic intestinal diseases are disorders caused by microscopic parasites that invade the gastrointestinal tract, specifically the small intestine. These parasites include protozoa (single-celled organisms) and helminths (parasitic worms). The most common protozoan parasites that cause intestinal disease are Giardia lamblia, Cryptosporidium parvum, and Entamoeba histolytica. Common helminthic parasites include roundworms (Ascaris lumbricoides), tapeworms (Taenia saginata and Taenia solium), hookworms (Ancylostoma duodenale and Necator americanus), and pinworms (Enterobius vermicularis).

Parasitic intestinal diseases can cause a variety of symptoms, including diarrhea, abdominal pain, bloating, nausea, vomiting, fatigue, and weight loss. The severity and duration of the symptoms depend on the type of parasite, the number of organisms present, and the immune status of the host.

Transmission of these parasites can occur through various routes, including contaminated food and water, person-to-person contact, and contact with contaminated soil or feces. Preventive measures include practicing good hygiene, washing hands thoroughly after using the toilet and before handling food, cooking food thoroughly, and avoiding consumption of raw or undercooked meat, poultry, or seafood.

Treatment of parasitic intestinal diseases typically involves the use of antiparasitic medications that target the specific parasite causing the infection. In some cases, supportive care such as fluid replacement and symptom management may also be necessary.

Protozoan infections are diseases caused by microscopic, single-celled organisms known as protozoa. These parasites can enter the human body through contaminated food, water, or contact with an infected person or animal. Once inside the body, they can multiply and cause a range of symptoms depending on the type of protozoan and where it infects in the body. Some common protozoan infections include malaria, giardiasis, amoebiasis, and toxoplasmosis. Symptoms can vary widely but may include diarrhea, abdominal pain, fever, fatigue, and skin rashes. Treatment typically involves the use of antiprotozoal medications to kill the parasites and alleviate symptoms.

Feces are the solid or semisolid remains of food that could not be digested or absorbed in the small intestine, along with bacteria and other waste products. After being stored in the colon, feces are eliminated from the body through the rectum and anus during defecation. Feces can vary in color, consistency, and odor depending on a person's diet, health status, and other factors.

A parasite is an organism that lives on or in a host organism and gets its sustenance at the expense of the host. Parasites are typically much smaller than their hosts, and they may be classified as either ectoparasites (which live on the outside of the host's body) or endoparasites (which live inside the host's body).

Parasites can cause a range of health problems in humans, depending on the type of parasite and the extent of the infection. Some parasites may cause only mild symptoms or none at all, while others can lead to serious illness or even death. Common symptoms of parasitic infections include diarrhea, abdominal pain, weight loss, and fatigue.

There are many different types of parasites that can infect humans, including protozoa (single-celled organisms), helminths (worms), and ectoparasites (such as lice and ticks). Parasitic infections are more common in developing countries with poor sanitation and hygiene, but they can also occur in industrialized nations.

Preventing parasitic infections typically involves practicing good hygiene, such as washing hands regularly, cooking food thoroughly, and avoiding contaminated water. Treatment for parasitic infections usually involves medication to kill the parasites and relieve symptoms.

Neale, G (1971). "Disaccharidase deficiencies". J Clin Pathol Suppl (R Coll Pathol). 5: 22-28. doi:10.1136/jcp.s3-5.1.22. PMC ... Disaccharidases are glycoside hydrolases, enzymes that break down certain types of sugars called disaccharides into simpler ... In the human body, disaccharidases are made mostly in an area of the small intestine's wall called the brush border, making ... Laws, J. W.; Spencer, J.; Neale, G. (1967). "Radiology in the diagnosis of disaccharidase deficiency". The British Journal of ...
Lentze MJ (June 2018). "The History of Maltose-active Disaccharidases". Journal of Pediatric Gastroenterology and Nutrition. 66 ...
Beldia) on small-intestinal disaccharidase activity in Wistar rats". Toxicology Reports. 5: 46-55. doi:10.1016/j.toxrep.2017.12 ...
Polysaccharidases and disaccharidases in the glycocalyx break down large sugar molecules, which are then absorbed. Glucose ...
This diagnostic method, called a disaccharidase assay, is conducted on tissue samples taken from the small intestine during an ... Puertolas MV, Fifi AC (2018). "The role of disaccharidase deficiencies in functional abdominal pain disorders-a narrative ... Hackenmueller SA, Grenache DG (2016). "Reference intervals for intestinal disaccharidase activities determined from a non- ...
Other disaccharidases In carnivorous plants digestive enzymes and acids break down insects and in some plants small animals. In ...
Each disaccharide is broken down with the help of a corresponding disaccharidase (sucrase, lactase, and maltase). There are two ... sugar into its two monosaccharides is accomplished by hydrolysis with the help of a type of enzyme called a disaccharidase. As ...
... disaccharidases MeSH D08.811.277.450.329.738 - sucrase MeSH D08.811.277.450.329.738.700 - sucrase-isomaltase complex MeSH ...
... apparently reduces activity of brush-border membrane disaccharidases, and possibly activates the calcium ion-dependent ...
... apparently reduces activity of brush-border membrane disaccharidases, and activates the calcium ion-dependent secretory ...
... functional consequences of bacterial infiltration cause enterocyte damage in the jejunum such as diminished disaccharidase ...
Other names in common use include isoflavonoid-7-O-beta[D-apiosyl-(1->6)-beta-D-glucoside], disaccharidase, isoflavonoid 7-O- ...
... by isolated small intestine of rats is via a specific saturable carrier in the absence of glucose and by the disaccharidase- ...
Enteric duplication cyst Situs inversus Cystic fibrosis Malrotation Persistent urachus Omphalocele Gastroschisis Disaccharidase ...
... especially among patients with a primary or secondary disaccharidase deficiency, such as lactose intolerance or sucrose ...
McArdle's disease Pompe's disease 271.1 Galactosemia 271.2 Hereditary fructose intolerance 271.3 Intestinal disaccharidase ...
Neale, G (1971). "Disaccharidase deficiencies". J Clin Pathol Suppl (R Coll Pathol). 5: 22-28. doi:10.1136/jcp.s3-5.1.22. PMC ... Disaccharidases are glycoside hydrolases, enzymes that break down certain types of sugars called disaccharides into simpler ... In the human body, disaccharidases are made mostly in an area of the small intestines wall called the brush border, making ... Laws, J. W.; Spencer, J.; Neale, G. (1967). "Radiology in the diagnosis of disaccharidase deficiency". The British Journal of ...
The aim of this study was to determine the influence of age on intestinal brush-border disaccharidases (lactase, sucrase, and ... L. Batičić, D. Detel i J. Varljen, "Age Dependent Changes in Activity of Intestinal Disaccharidases and Alkaline Phosphatase ... Batičić, L., Detel, D. i Varljen, J. (2008). Age Dependent Changes in Activity of Intestinal Disaccharidases and Alkaline ... Batičić, L., Detel, D., i Varljen, J. (2008). Age Dependent Changes in Activity of Intestinal Disaccharidases and Alkaline ...
... may prevent digestive problems caused by a deficiency in disaccharidases and oxidative stress-related diseases. The study has ... Tagged Under: alternative medicine, antioxidant, disaccharidase deficiency, functional food, herbal medicine, Herbs, lactose ... The researchers suggest that pineapple guava is particularly beneficial to disaccharidases deficit and as an adjuvant treatment ... FRUIT EXERTS ANTIOXIDANT PROPERTIES AND MODULATES DISACCHARIDASES ACTIVITIES IN HUMAN INTESTINAL EPITHELIAL CELLS. Phytotherapy ...
Reversing non-congenital disaccharidase deficiency is something that can often be accomplished by paying careful attention ... If you have been diagnosed with disaccharidase deficiency and told that you need to avoid all lactose, maltose and/or sucrose, ... Disaccharidase Diet - Elimination Diet. If you are going to go on a disaccharidase diet, the most important clinical aspect is ... Disaccharidase Deficiency Causes and Natural Treatment. 1 Comment / Articles, Conditions / By Dr. Houston C. Anderson, DC, MS ...
Weight loss, disaccharidase deficiency, malabsorption, and growth retardation are possible complications. [51, 52] G ... Giardia- induced loss of intestinal brush border surface area, villus flattening, inhibition of disaccharidase activities, and ... the reduction in disaccharidase activities, and the more pronounced abnormalities of villous architecture that are seen in ...
Disaccharidase Sucrose (table sugar, cane sugar, saccharose, or beet sugar). glucose. fructose. α(1→2). sucrase ...
carbohydrates by amylases and membrane-bound disaccharidases. *lipids by lipase, including the action of bile salts ...
Sugar-dependent selective induction of mouse jejunal disaccharidase activities. Collins, A.J., James, P.S., Smith, M.W. J. ... Sugar-dependent selective induction of mouse jejunal disaccharidase activities.. 1. Sugar-containing diets chosen not to affect ... been fed to mice previously maintained on a low carbohydrate diet in order to determine their ability to induce disaccharidase ...
Intestinal disaccharidase activities in relation to age, race, and mucosal damage. Gastroenterology. 1978;75(5):847-55. pmid: ...
Routine disaccharidase testing: are we there yet?. Current Opinion in Gastroenterology 2020; 36(2): 101 doi: 10.1097/MOG. ...
Lactase is a disaccharidase present on the surface of mammalian small intestinal mucosal microvilli, and many beneficial ... Lactase is a disaccharidase present on the surface of mammalian small intestinal mucosal microvilli, and many beneficial ... Lactase is a disaccharidase present on the surface of the small intestinal mucosa of mammals. It is distributed in foci in the ...
Effect of severe zinc deficiency on activity of intestinal disaccharidases and 3-hydroxy-3-methyl-glutaryl coenzyme A reductase ...
Measurement of disaccharidase activity of intestine 443420006. *Measurement of girth 54983001. *Measurement of interstitial ...
Acetic acid suppresses the increase in disaccharidase activity that occurs during culture of caco-2 cells. J. Nutr. 2000, 130, ... which has been demonstrated to reduce the digestive capacity of disaccharidases in vitro [7] and to enhance the clearance of ...
It inhibited disaccharidases activities and decreased glucose transportation cross the intestinal epithelium [15, 16]. This may ...
Disaccharidase activity in children with inflammatory bowel disease. Turk J Gastroenterol 2014;25:185-91.doi:10.5152/tjg. ...
An automated method for the determination of intestinal disaccharidase and glucoamylase activities; Journal of Automated ...
the activity of intestinal lipase, disaccharidases sucrase and maltase enzymes [27]. In another study, Platel K and Srinivasan ...
Effects of the intestinal flagellate, Cochlosoma anatis, on intestinal mucosal morphology and disaccharidase activity in ...
Disaccharidase Activity in the Small Intestine of Susceptible and Resistant Mice after Primary and Challenge Infections with ...
tropical sprue, disaccharidase deficiency, and pancreatic insufficiency) and weight loss (cancer, chronic malabsorption). ... In patients with disaccharidase deficiencies (most commonly lactase deficiency), large amounts of disaccharides pass into the ...
bottom - enteorcytes -, secrete Disaccharidases and peptidases are secreted by the absorptive cells ...
Modulatory effect of fenugreek seed mucilage and spent turmeric on intestinal and renal disaccharidases in streptozotocin ... lowers carbohydrate digestion and absorption and can modulate the activities of kidney and intestinal disaccharidases, possibly ...
Inhibitory effects of mulberry fruit on intestinal disaccharidase activity and hyperglycemia in streptozotocin-induced diabetic ...
... and disaccharidase deficiencies, which can lead to osmotic diarrhea, particularly after consuming large amounts of fructose, ...
Galactosuria 271.2 Hereditary fructose intolerance Essential benign fructosuria Fructosemia 271.3 Intestinal disaccharidase ...
... and sometimes depressed disaccharidases (maltase, sucrase, lactase).Footnote 6 Footnote 28 Footnote 30 Stimulation of the ...
3232A Metabolic Powder, for Infants & Children with Disaccharidase deficiencies. *BCAD 1 Metabolic Powder, for Infants & ...
  • Disaccharidases are glycoside hydrolases, enzymes that break down certain types of sugars called disaccharides into simpler sugars called monosaccharides. (wikipedia.org)
  • Enzymes with DPP-IV activity and a full range of disaccharidases are included. (purelykids.com)
  • Berberine also helps block the digestion of carbohydrates, including starch, by inhibiting disaccharidases - the enzymes needed to break them down. (twofarmkids.com)
  • This could be achieved through the inhibition of carbohydrate hydrolysing enzymes, such as salivary and pancreatic amylases, and intestinal disaccharidases, α-glucosidase, β-galactosidase, and β-fructofuronosidase (invertase). (springeropen.com)
  • S. boulardii increases the activities of intestinal brush border enzymes such as disaccharidases, a-glucosidases, alkaline phosphatases, and aminopeptidases. (klaire.com)
  • Bodily enzymes known as disaccharidases affect blood sugar. (vshred.com)
  • Disaccharidase deficiency in infants with cow's milk protein intolerance. (wikipedia.org)
  • If you have been diagnosed with disaccharidase deficiency and told that you need to avoid all lactose, maltose and/or sucrose, and you have been told your days of enjoying almost any food are all over, often this is not the case. (drhoustonanderson.com)
  • Reversing non-congenital disaccharidase deficiency is something that can often be accomplished by paying careful attention to your symptoms and making necessary lifestyle changes. (drhoustonanderson.com)
  • Being born with disaccharidase deficiency is very rare. (drhoustonanderson.com)
  • So, if you made it past the first few years of life without having debilitating disaccharidase deficiency, then you stand a great chance to be able to recover if you have developed the condition later in life. (drhoustonanderson.com)
  • A study published in the journal Phytotherapy Research has found that extracts from pineapple guava ( Feijoa sellowiana ) may prevent digestive problems caused by a deficiency in disaccharidases and oxidative stress-related diseases. (nutrients.news)
  • Disaccharidase deficiency is defined as an enzyme activity of at least two standard deviations below the normal mean value. (mhmedical.com)
  • Lactase (breaks down lactose into glucose and galactose) Maltase (breaks down maltose into 2 glucoses) Sucrase (breaks down sucrose into glucose and fructose) Trehalase (breaks down trehalose into 2 glucoses) For a thorough scientific overview of small-intestinal disaccharidases, one can consult chapter 75 of OMMBID. (wikipedia.org)
  • The aim of this study was to determine the influence of age on intestinal brush-border disaccharidases (lactase, sucrase, and maltase), and alkaline phosphatase activity in CD26 deficient mice. (srce.hr)
  • Lactase is a disaccharidase present on the surface of mammalian small intestinal mucosal microvilli, and many beneficial intestinal bacteria have the ability to produce lactase. (selfgrowth.com)
  • Lactase is a disaccharidase present on the surface of the small intestinal mucosa of mammals. (selfgrowth.com)
  • According to Pierre Russo in Surgical Pathology of the GI Tract, Liver, Biliary Tract and Pancreas (2nd Edition, 2009), disaccharidase deficiencies are "often secondary, resulting from diffuse mucosal damage caused by infectious gastroenteritis, gluten-sensitive enteropathy, or other food allergies. (drhoustonanderson.com)
  • Effects of the intestinal flagellate, Cochlosoma anatis, on intestinal mucosal morphology and disaccharidase activity in Muscovy ducklings. (semanticscholar.org)
  • Characterization of Mucosal Disaccharidases from Human Intestine. (churup.com)
  • Clinical presentation, oral tolerance test with the corresponding disaccharides, sucrose breath hydrogen test, differential urinary disaccharide excretion, and measurement of intestinal disaccharidase activity in a small intestine biopsy lead to the diagnosis. (mhmedical.com)
  • SA Pathology has developed a new test information sheet regarding disaccharidase testing collection and transport to ensure high quality biopsy specimens are provided for testing. (countrysaphn.com.au)
  • Researchers at Federico II University of Naples and La Sapienza University of Rome in Italy examined the effects of pineapple guava extract on the viability, membrane peroxidation, disaccharidase activities and proliferation of in vitro models of human intestinal epithelial cells. (nutrients.news)
  • Sugar-dependent selective induction of mouse jejunal disaccharidase activities. (wikigenes.org)
  • Intestinal disaccharidase activity and glucose absorption were decreased and gastrointestinal motility increased by the SDF fraction. (nih.gov)
  • It shows complete association with intestinal disaccharidase activity, with the genotype CC −13 910 meaning adult-type hypolactasia (primary LM) and the genotypes CT −13 910 and TT −13 910 lactose absorption. (nature.com)
  • Effect on carbohydrate break down was assayed using intestinal disaccharidase enzyme, α-amylase inhibition assays and Six-Segment study of the GI tract. (biomedcentral.com)
  • The extract was also found to inhibit action of both intestinal disaccharidase and α-amylase. (biomedcentral.com)
  • Intestinal disaccharidase and dipeptidase activities were measured in mucosal biopsies from the proximal jejunum in 20 patients with Crohn's disease apparently confined to the distal ileum or large bowel, 14 patients with ulcerative colitis, and 14 healthy volunteers who acted as controls. (bmj.com)
  • Lactase (breaks down lactose into glucose and galactose) Maltase (breaks down maltose into 2 glucoses) Sucrase (breaks down sucrose into glucose and fructose) Trehalase (breaks down trehalose into 2 glucoses) For a thorough scientific overview of small-intestinal disaccharidases, one can consult chapter 75 of OMMBID. (wikipedia.org)
  • Lactose intolerance is the most common problem of carbohydrate digestion and is created by an insufficient amount of lactase (a disaccharidase) enzyme, which is used to break down the sugar. (wikidoc.org)
  • A few disaccharides can be pinocytosed and hydrolyzed to monosaccharides by disaccharidases. (brainkart.com)
  • The proposed action mechanism may involve interference in the absorption of carbohydrates through inhibition of intestinal disaccharidases and glucose transportation. (hindawi.com)
  • 13. Disaccharidases, leucine aminopeptidase, and glucose uptake in intestinalized gastric mucosa and in gastric carcinoma. (nih.gov)
  • This study was carried out to investigate the effects of tributyrin (TB) on the growth performance, pro-inflammatory cytokines, intestinal morphology, energy status, disaccharidase activity, and antioxidative capacity of broilers challenged with lipopolysaccharide (LPS). (animbiosci.org)
  • Further studies that can be performed to determine the specific carbohydrate that is being malabsorbed include esophagogastroduodenoscopy (EGD) with histology and additional duodenal biopsies for determination of disaccharidase levels, and rarely electron microscopy as well as other carbohydrate-specific hydrogen breath tests (lactose, sucrose, fructose, and maltose). (medscape.com)
  • 4. Disaccharidases of the gastric mucosa in chronic atrophic gastritis with intestinal metaplasia. (nih.gov)
  • Polysaccharidases and disaccharidases in the glycocalyx break down large sugar molecules, which are then absorbed. (wikidoc.org)