Oligo-1,6-Glucosidase
alpha-Glucosidases
1-Deoxynojirimycin
Polyisoprenyl Phosphate Oligosaccharides
Oligosaccharides
Swainsonine
beta-Glucosidase
Calnexin
Alkaloids
Glycoproteins
Substrate Specificity
Endoplasmic Reticulum
Glycosylation
alpha 1-Antitrypsin
Molecular Sequence Data
Chromatography, Gel
Receptors, Adrenergic, alpha
Hypoxia-Inducible Factor 1, alpha Subunit
alpha7 Nicotinic Acetylcholine Receptor
Integrin alpha3beta1
Integrin alpha4
Integrin alpha6
Integrin alpha5beta1
Integrin alpha4beta1
Interleukin-1alpha
Integrin alpha2beta1
Receptors, Adrenergic, alpha-1
Integrin alpha5
Integrin alpha1beta1
Receptors, Adrenergic, alpha-2
Integrin alpha6beta1
Base Sequence
Integrin alpha6beta4
Integrin alpha Chains
Integrins
Integrin alpha1
Alpha Rhythm
Integrin alpha3
alpha 1-Antitrypsin Deficiency
Protein Binding
Receptors, Nicotinic
PPAR alpha
Dinoprost
Adrenergic alpha-Antagonists
Hepatocyte Nuclear Factor 1-alpha
Binding Sites
Alternative splicing of transcripts encoding the alpha- and beta-subunits of mouse glucosidase II in T lymphocytes. (1/973)
Glucosidase II is a processing enzyme of the endoplasmic reticulum that functions to hydrolyze two glucose residues in immature N -linked oligosaccharides attached to newly synthesized polypeptides. We previously reported the cDNA cloning of the alpha- and beta-subunits of mouse glucosidase II from T cells following copurification of these proteins with the highly glycosylated transmembrane protein-tyrosine phosphatase CD45. Subsequent examination of additional cDNA clones, coupled with partial genomic DNA sequencing, has revealed that both subunits are encoded by gene products that undergo alternative splicing in T lymphocytes. The catalytic alpha-subunit possesses two variably expressed segments, box Alpha1, consisting of 22 amino acids located proximal to the amino-terminus, and box Alpha2, composed of 9 amino acids situated between the amino-terminus and the putative catalytic site in the central region of the molecule. Box Beta1, a variably expressed 7 amino acid segment in the beta-subunit of glucosidase II, is located immediately downstream of an acidic stretch near the carboxyl-terminus. Screening of reverse transcribed RNA by polymerase chain reaction confirms the variable inclusion of each of these segments in transcripts obtained from a panel of T-lymphocyte cell lines. Thus, distinct isoforms of glucosidase II exist that may perform specialized functions. (+info)The AcbC protein from Actinoplanes species is a C7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the alpha-glucosidase inhibitor acarbose. (2/973)
The putative biosynthetic gene cluster for the alpha-glucosidase inhibitor acarbose was identified in the producer Actinoplanes sp. 50/110 by cloning a DNA segment containing the conserved gene for dTDP-D-glucose 4,6-dehydratase, acbB. The two flanking genes were acbA (dTDP-D-glucose synthase) and acbC, encoding a protein with significant similarity to 3-dehydroquinate synthases (AroB proteins). The acbC gene was overexpressed heterologously in Streptomyces lividans 66, and the product was shown to be a C7-cyclitol synthase using sedo-heptulose 7-phosphate, but not ido-heptulose 7-phosphate, as its substrate. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety of acarbose. A possible five-step reaction mechanism is proposed for the cyclization reaction catalyzed by AcbC based on the recent analysis of the three-dimensional structure of a eukaryotic 3-dehydroquinate synthase domain (Carpenter, E. P., Hawkins, A. R., Frost, J. W., and Brown, K. A. (1998) Nature 394, 299-302). (+info)Trypanosoma cruzi calreticulin is a lectin that binds monoglucosylated oligosaccharides but not protein moieties of glycoproteins. (3/973)
Trypanosoma cruzi is a protozoan parasite that belongs to an early branch in evolution. Although it lacks several features of the pathway of protein N-glycosylation and oligosaccharide processing present in the endoplasmic reticulum of higher eukaryotes, it displays UDP-Glc:glycoprotein glucosyltransferase and glucosidase II activities. It is herewith reported that this protozoan also expresses a calreticulin-like molecule, the third component of the quality control of glycoprotein folding. No calnexin-encoding gene was detected. Recombinant T. cruzi calreticulin specifically recognized free monoglucosylated high-mannose-type oligosaccharides. Addition of anti-calreticulin serum to extracts obtained from cells pulse-chased with [35S]Met plus [35S]Cys immunoprecipitated two proteins that were identified as calreticulin and the lysosomal proteinase cruzipain (a major soluble glycoprotein). The latter but not the former protein disappeared from immunoprecipitates upon chasing cells. Contrary to what happens in mammalian cells, addition of the glucosidase II inhibitor 1-deoxynojirimycin promoted calreticulin-cruzipain interaction. This result is consistent with the known pathway of protein N-glycosylation and oligosaccharide processing occurring in T. cruzi. A treatment of the calreticulin-cruzipain complexes with endo-beta-N-acetylglucosaminidase H either before or after addition of anti-calreticulin serum completely disrupted calreticulin-cruzipain interaction. In addition, mature monoglucosylated but not unglucosylated cruzipain isolated from lysosomes was found to interact with recombinant calreticulin. It was concluded that the quality control of glycoprotein folding appeared early in evolution, and that T. cruzi calreticulin binds monoglucosylated oligosaccharides but not the protein moiety of cruzipain. Furthermore, evidence is presented indicating that glucosyltransferase glucosylated cruzipain at its last folding stages. (+info)Murine acid alpha-glucosidase: cell-specific mRNA differential expression during development and maturation. (4/973)
Acid alpha-glucosidase (GAA) cleaves the alpha1-4 and alpha1-6 glycosidic linkages of glycogen and related alpha-glucosyl substrates within lysosomes. Its deficiency results in glycogen storage disease type II (GSDII) variants including Pompe disease. To gain insight into the tissue patterns of involvement by glycogen storage in GSDII, GAA mRNA expression in mouse tissues was evaluated by Northern blot and in situ hybridization analyses. Extensive temporal and spatial variation of GAA mRNA was observed. During preterm maturation, GAA mRNA levels of whole mice progressively increased as assessed by Northern analysis. By in situ hybridization with GAA antisense mRNA, low signals were detected in most tissues throughout gestation. However, increased expression in specific cell types of different tissues was observed beginning at 16 days post coitum in developing brain neurons, primitive inner ear cells, and seminiferous tubular epithelium. In adult mice, whole-organ GAA mRNA levels were highest in brain, moderate in heart, liver, and skeletal muscle, and lowest in the series kidney > lung > testis > spleen. By in situ hybridization, the highest-intensity signals were in neurons of the central and peripheral nervous systems whereas neuroglial cells had only low-level signal. Signals of moderate intensity were in cardiomyocytes whereas low signals were in hepatocytes and skeletal muscle myocytes and very low in cells of the lungs, thymus, pancreas, spleen, and adrenal glands. However, testicular Sertoli cells and kidney tubular epithelial cells had significant signals even though surrounding cells had very low signals. The discrete temporal and spatial variations of GAA mRNA during development indicate different physiological roles for this enzyme in various cell types and developmental stages. (+info)Delayed symptom onset and increased life expectancy in Sandhoff disease mice treated with N-butyldeoxynojirimycin. (5/973)
Sandhoff disease is a neurodegenerative disorder resulting from the autosomal recessive inheritance of mutations in the HEXB gene, which encodes the beta-subunit of beta-hexosaminidase. GM2 ganglioside fails to be degraded and accumulates within lysosomes in cells of the periphery and the central nervous system (CNS). There are currently no therapies for the glycosphingolipid lysosomal storage diseases that involve CNS pathology, including the GM2 gangliosidoses. One strategy for treating this and related diseases is substrate deprivation. This would utilize an inhibitor of glycosphingolipid biosynthesis to balance synthesis with the impaired rate of catabolism, thus preventing storage. One such inhibitor is N-butyldeoxynojirimycin, which currently is in clinical trials for the potential treatment of type 1 Gaucher disease, a related disease that involves glycosphingolipid storage in peripheral tissues, but not in the CNS. In this study, we have evaluated whether this drug also could be applied to the treatment of diseases with CNS storage and pathology. We therefore have treated a mouse model of Sandhoff disease with the inhibitor N-butyldeoxynojirimycin. The treated mice have delayed symptom onset, reduced storage in the brain and peripheral tissues, and increased life expectancy. Substrate deprivation therefore offers a potentially general therapy for this family of lysosomal storage diseases, including those with CNS disease. (+info)Androgen regulation of glycosidase secretion in epithelial cell cultures from human epididymis. (6/973)
The human epididymis and its secretions actively promote sperm fertilizing capacity and provide protection for spermatozoa against harmful influences. Among epididymal secretions, glycosidases have been recently studied and associated with molecular changes on the sperm surface. In the present work, we studied the influence of different concentrations of testosterone, dihydrotestosterone and cyproterone acetate on the secretion of alpha-glucosidase, N-acetyl-glucosaminidase, beta-glucuronidase and alpha-mannosidase by isolated and cultured epithelial cells from human caput, corpus and cauda epididymides. Cell cultures were obtained from aggregates of isolated tubule fragments plated on extracellular matrix-covered multi-well plates. Activities of the glycosidases were measured in conditioned culture media and were higher in the distal regions of the epididymis. Testosterone and dihydrotestosterone significantly increase the enzyme secretion in a concentration-dependent manner. This increase was higher in corpus and/or cauda than in caput epididymis. Cyproterone acetate caused a dose-dependent decrease in glycosidase secretion in cultures from all epididymal regions. It is concluded that the secretion of epididymal glycosidases is regulated by androgen, being stimulated by dihydrotestosterone and testosterone and inhibited by the androgen antagonist cyproterone acetate. (+info)Coordinate transcriptional control in the hyperthermophilic archaeon Sulfolobus solfataricus. (7/973)
The existence of a global gene regulatory system in the hyperthermophilic archaeon Sulfolobus solfataricus is described. The system is responsive to carbon source quality and acts at the level of transcription to coordinate synthesis of three physically unlinked glycosyl hydrolases implicated in carbohydrate utilization. The specific activities of three enzymes, an alpha-glucosidase (malA), a beta-glycosidase (lacS), and an alpha-amylase, were reduced 4-, 20-, and 10-fold, respectively, in response to the addition of supplementary carbon sources to a minimal sucrose medium. Western blot analysis using anti-alpha-glucosidase and anti-beta-glycosidase antibodies indicated that reduced enzyme activities resulted exclusively from decreased enzyme levels. Northern blot analysis of malA and lacS mRNAs revealed that changes in enzyme abundance arose primarily from reductions in transcript concentrations. Culture conditions precipitating rapid changes in lacS gene expression were established to determine the response time of the regulatory system in vivo. Full induction occurred within a single generation whereas full repression occurred more slowly, requiring nearly 38 generations. Since lacS mRNA abundance changed much more rapidly in response to a nutrient down shift than to a nutrient up shift, transcript synthesis rather than degradation likely plays a role in the regulatory response. (+info)Purification and characterization of an alpha-glucosidase from Rhizobium sp. (Robinia pseudoacacia L.) strain USDA 4280. (8/973)
A novel alpha-glucosidase with an apparent subunit mass of 59 +/- 0. 5 kDa was purified from protein extracts of Rhizobium sp. strain USDA 4280, a nodulating strain of black locust (Robinia pseudoacacia L), and characterized. After purification to homogeneity (475-fold; yield, 18%) by ammonium sulfate precipitation, cation-exchange chromatography, hydrophobic chromatography, dye chromatography, and gel filtration, this enzyme had a pI of 4.75 +/- 0.05. The enzyme activity was optimal at pH 6.0 to 6.5 and 35 degrees C. The activity increased in the presence of NH4+ and K+ ions but was inhibited by Cu2+, Ag+, Hg+, and Fe2+ ions and by various phenyl, phenol, and flavonoid derivatives. Native enzyme activity was revealed by native gel electrophoresis and isoelectrofocusing-polyacrylamide gel electrophoresis with fluorescence detection in which 4-methylumbelliferyl alpha-glucoside was the fluorogenic substrate. The enzyme was more active with alpha-glucosides substituted with aromatic aglycones than with oligosaccharides. This alpha-glucosidase exhibited Michaelis-Menten kinetics with 4-methylumbelliferyl alpha-D-glucopyranoside (Km, 0.141 microM; Vmax, 6.79 micromol min-1 mg-1) and with p-nitrophenyl alpha-D-glucopyranoside (Km, 0.037 microM; Vmax, 2.92 micromol min-1 mg-1). Maltose, trehalose, and sucrose were also hydrolyzed by this enzyme. (+info)People with AATD have low levels of functional AAT in their blood, which can lead to premature lung disease and liver disease. The most common form of AATD is caused by the Pi*Z phenotype, which results from a missense mutation in the SERPINA1 gene. This mutation leads to misfolding and accumulation of AAT in the liver, where it is normally broken down and secreted into the bloodstream.
The most common symptoms of AATD are:
* Chronic obstructive pulmonary disease (COPD)
* Emphysema
* Lung fibrosis
* Liver cirrhosis
* Gallstones
The diagnosis of AATD is based on a combination of clinical symptoms, laboratory tests, and genetic analysis. Treatment for AATD typically involves managing the underlying symptoms and preventing complications. For example, individuals with COPD may receive bronchodilators and corticosteroids to help improve lung function and reduce inflammation. Liver disease may be treated with medications to slow the progression of cirrhosis or with liver transplantation in severe cases.
The goal of genetic counseling for AATD is to provide information about the risk of transmitting the disorder to offspring and to discuss options for prenatal testing and family planning. Prenatal testing can be performed on a fetus by analyzing a sample of cells from the placenta or amniotic fluid. Carrier testing can also be performed in individuals who have a family history of AATD.
The prognosis for AATD varies depending on the severity of the mutation and the specific symptoms present. With appropriate management, many individuals with AATD can lead active and productive lives. However, the disorder can be severe and life-threatening in some cases, especially if left untreated or if there is a delay in diagnosis.
Currently, there is no cure for AATD, and treatment is focused on managing symptoms and preventing complications. However, research into the genetics of AATD is ongoing, and new developments in gene therapy and other areas may provide hope for improved treatments and outcomes in the future.
Alpha-glucosidase
Glucan endo-1,3-alpha-glucosidase
Lysosomal alpha-glucosidase
Acid alpha-glucosidase
Sucrose alpha-glucosidase
Alpha-glucosidase inhibitor
Amylo-alpha-1,6-glucosidase
Glucan 1,3-alpha-glucosidase
Branched-dextran exo-1,2-alpha-glucosidase
Hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase
Maltose-6'-phosphate glucosidase
Protein-glucosylgalactosylhydroxylysine glucosidase
Mannosyl-oligosaccharide glucosidase
Enzyme replacement therapy
Glucosidases
Glycoside hydrolase family 31
GANC
Glycoside hydrolase family 15
GANAB
Voglibose
Maltase-glucoamylase
Glucan 1,6-a-glucosidase
Glycogen debranching enzyme
Trefoil knot fold
Glycoside hydrolase family 4
Maltase
Diplazium esculentum
Miglitol
Polycystic kidney disease 3 (autosomal dominant)
Streptomyces galbus
Naringinase
Angelicin
Lipid signaling
Glycogen phosphorylase
Malbranchea cinnamomea
Chebulagic acid
Glycosidic bond
Actinoplanes utahensis
Inborn errors of metabolism
GCS1
Pseudogymnoascus destructans
Cellulase
Acarviosin
Indigestion
MAPK13
Inulinase
Hypoglycemia
Alpha-D-xyloside xylohydrolase
17α-Estradiol
Structural bioinformatics
Hypospermia
Snodgrassella alvi
Sucrase
DailyMed - Search Results for alpha-Glucosidase Inhibitor
Alpha-glucosidase inhibitors: MedlinePlus Medical Encyclopedia Image
Alpha Glucosidase Inhibitors - PubMed
Alpha Glucosidase Inhibitors - PubMed
Pediatric Type 2 Diabetes Mellitus Medication: Biguanides, Sulfonylureas, Meglitinides, Alpha-glucosidase inhibitors,...
Pediatric Type 2 Diabetes Mellitus Medication: Biguanides, Sulfonylureas, Meglitinides, Alpha-glucosidase inhibitors,...
Lysosomal Alpha Glucosidase (GAA) Antibody - Connecting Americans to Their Personal Health Care
Inhibition of cellular alpha-glucosidases results in increased presentation of hepatitis B virus glycoprotein-derived peptides...
acid alpha-glucosidase
Subjects: alpha-Glucosidases - Digital Collections - National Library of Medicine Search Results
DailyMed - Search Results for alpha Glucosidase Inhibitors
Global Alpha Glucosidase Inhibitors - Market Analysis | Size
Alpha-Glucosidase - DNA Ligase Inhibitors with Broad-Spectrum Activity
Pancreatic lipase and alpha-glucosidase inhibitors screening from Schisandra chinensis based on spectrum-effect relationship...
Alpha-glucosidase activity in four varieties of Fiji sugar cane - USP Electronic Research Repository
Novel Methods and Data Sources for Surveillance of State-Level Diabetes and Prediabetes Prevalence
Design, synthesis, ADME prediction and anti-hyperglycemic evaluation of new alkoxyimino-substituted phenyl carboxylic acids as...
Materials | Free Full-Text | A Review on Plant-Mediated Synthesis of Bimetallic Nanoparticles, Characterisation and Their...
Invokana: Side effects, dosage, alternatives, uses, and more
Intracranial Aneurysms Guide: Causes, Symptoms and Treatment Options
Microwave Assistant Synthesis of Novel Inhibitors of Lipase, Alpha-Glucosidase and Antimicrobial Activities Based on...
Pompe disease: MedlinePlus Genetics
MedlinePlus - Search Results for: ACARBOSE
Creator: Halvorson, Harlyn O. - Sol Spiegelman - Profiles in Science Search Results
Publication Detail
Diovan (valsartan) dose, indications, adverse effects, interactions... from PDR.net
MMRRC:044343-MU
1u8x.1 | SWISS-MODEL Template Library
Inhibitors21
- Alpha-glucosidase inhibitors (such as acarbose) decrease the absorption of carbohydrates from the digestive tract, thereby lowering the after-meal glucose levels. (medlineplus.gov)
- Alpha glucosidase inhibitors have been shown to be effective in improving glycemic control in type 2 diabetes. (nih.gov)
- Two alpha glucosidase inhibitors have been approved for use in the United States, acarbose (Precose) in 1995 and miglitol (Glyset) in 1996. (nih.gov)
- Inhibitors of alpha glucosidases prevent the trimming of oligosaccharides on certain nascent glycoproteins, including the hepatitis B virus MHBs envelope glycoprotein. (nih.gov)
- Using either a model epitope, or a natural MHBs epitope, it was demonstrated that glucosidase inhibitors enhanced presentation by MHC class I and promoted activation of antigen-specific CTLs, suggesting a pharmacologic approach to immune modulation. (nih.gov)
- The Global Alpha-Glucosidase Inhibitors market is expected to grow at a moderate CAGR during the forecast period. (globalmarketestimates.com)
- Rise in the geriatric population in emerging economies in the Asia Pacific region is likely to further boost the market for Alpha-Glucosidase Inhibitors. (globalmarketestimates.com)
- The market for Alpha-Glucosidase Inhibitors is expected to be larger in areas with high carbohydrate consumption. (globalmarketestimates.com)
- However, Alpha-Glucosidase Inhibitors are used as a second line monotherapy treatment or are used in combination with first-line therapy drugs. (globalmarketestimates.com)
- On the basis of disease type, the Alpha-Glucosidase Inhibitors market can be segmented into type-1 and type-2 diabetes. (globalmarketestimates.com)
- Use of Alpha-Glucosidase Inhibitors is higher in the treatment of type-2 diabetes and is therefore projected to hold the higher market share in terms of revenue. (globalmarketestimates.com)
- The Global Alpha-Glucosidase Inhibitors market is segmented into Online Pharmacies, Retail Pharmacies, and Hospital Pharmacies based on the distribution channel. (globalmarketestimates.com)
- The Asia Pacific market for Alpha-Glucosidase Inhibitors is projected to grow at the highest CAGR owing to a demonstrated rise in geriatric population over the past few years along with a rise in cases of type-2 diabetes. (globalmarketestimates.com)
- The North American region is likely to hold the larger market share in the Alpha-Glucosidase Inhibitors Market owing to technological advancements and easy availability of the drug in medical facilities. (globalmarketestimates.com)
- The market for Alpha-Glucosidase Inhibitors in Central & South America is also expected to grow at a significant rate due to initiatives were taken by the Government to use advanced drugs for diabetes treatment. (globalmarketestimates.com)
- Pancreatic lipase and alpha-glucosidase inhibitors screening from Schisandra chinensis based on spectrum-effect relationship and ultra-high-performance liquid chromatography-tandem mass spectrometry. (bvsalud.org)
- Grape seed and tea extracts and catechin 3-gallates are potent inhibitors of α-amylase and α-glucosidase activity. (nih.gov)
- Whereas tea extracts and catechin 3-gallates were less effective inhibitors of α-amylase, they were potent inhibitors of α-glucosidase. (nih.gov)
- The data show that plant extracts containing catechin 3-gallates, in particular epigallocatechin gallate, are potent inhibitors of α-glucosidase activity and suggest that procyanidins in grape seed extract strongly inhibit α-amylase activity. (nih.gov)
- 11. Identification of alpha-glucosidase inhibitors from a new fermented tea obtained by tea-rolling processing of loquat (Eriobotrya japonica) and green tea leaves. (nih.gov)
- For example, pu- erh contains alpha-amylase and alpha-glucosidase inhibitors that reduce the absorption of dietary glucose and lower blood glucose levels, particularly after eating. (marksdailyapple.com)
Inhibition8
- Inhibition of cellular alpha-glucosidases results in increased presentation of hepatitis B virus glycoprotein-derived peptides by MHC class I. (nih.gov)
- As peptides loaded onto newly synthesized MHC class I complexes are predominantly derived from proteasomes, the possibility that glucosidase inhibition could increase presentation by MHC class I was determined. (nih.gov)
- The half-maximal inhibition concentration values for pancreatic lipase and alpha-glucosidase inhibition were separately measured by enzymatic reactions. (bvsalud.org)
- Based on the inhibition percentage, the inhibition activity of 102 and 105 on a -glucosidase had higher potential than a -amylase. (thesciencein.org)
- To evaluate the relative potency of extracts and catechins, their concentrations required for 50 and 90% inhibition of enzyme activity were determined and compared to the widely used pharmacological glucosidase inhibitor, acarbose. (nih.gov)
- 3. Luteolin, a flavone, does not suppress postprandial glucose absorption through an inhibition of alpha-glucosidase action. (nih.gov)
- 13. Antidiabetic activity of lipophilic (-)-epigallocatechin-3-gallate derivative under its role of alpha-glucosidase inhibition. (nih.gov)
- The antihyperglycemic action of acarbose results from a competitive, reversible inhibition of pancreatic alpha-amylase and membrane-bound intestinal alpha-glucoside hydrolase enzymes. (nih.gov)
Inhibitory8
- In this study, the active components of Schisandra chinensis responsible for pancreatic lipase and alpha-glucosidase inhibitory activity were screened and identified based on a spectrum-effect relationship study in combination with ultra-performance liquid chromatography - tandem mass spectrometry analysis . (bvsalud.org)
- In an attempt to further explore the role of substituted carboxylic acid derivatives as antidiabetic agent, a series of alkoxyimino-substituted carboxylic acid derivatives ( 101-206 ) were designed, synthesized and evaluated for their inhibitory potential against a -amylase and a -glucosidase enzyme. (thesciencein.org)
- This study evaluated the inhibitory effects of plant-based extracts (grape seed, green tea, and white tea) and their constituent flavan-3-ol monomers (catechins) on α-amylase and α-glucosidase activity, two key glucosidases required for starch digestion in humans. (nih.gov)
- 1. alpha-Glucosidase inhibitory profile of catechins and theaflavins. (nih.gov)
- 9. alpha-Glucosidase inhibitory activity of some Sri Lanka plant extracts, one of which, Cassia auriculata, exerts a strong antihyperglycemic effect in rats comparable to the therapeutic drug acarbose. (nih.gov)
- One metabolite (formed by cleavage of a glucose molecule from acarbose) also has alpha-glucosidase inhibitory activity. (nih.gov)
- 2) Antidiabetic function has been attributed to α -glucosidase inhibitory activity. (stuartxchange.com)
- Study showed the methanolic extract from the stems of Salacia chinensis showed potent anti-hyperglycemic effects in oral sucrose or maltose-loaded rats, inhibitory effects on intestinal α-glucosidase, rat lens aldose reductase and radical scavenging activities. (stuartxchange.com)
Enzyme13
- Alpha glucosidase is an intestinal brush border enzyme responsible for the hydrolysis of disaccharides which is necessary for the absorption of starch, dextrins and disaccharides. (nih.gov)
- Without enough of this enzyme, called acid alpha-glucosidase (GAA), glycogen can accumulate destructively in the liver, heart, and skeletal muscles, making it increasingly difficult to walk, eat, and even breathe. (nih.gov)
- The mode of binding interactions between the a -glucosidase enzyme and the compound 102 was established to be uncompetitive using kinetic analysis. (thesciencein.org)
- The GAA gene provides instructions for producing an enzyme called acid alpha-glucosidase (also known as acid maltase). (nih.gov)
- Pompe disease is a rare, inherited disorder characterized by the deficiency of an enzyme called acid alpha-glucosidase (GAA). (nih.gov)
- glucosidase as adjuvant enzyme(s) for .alpha. (justia.com)
- glucosidase as an adjuvant enzyme needs to immediately decompose the maltooligosaccharide produced by .alpha. (justia.com)
- When the enzyme is kept in contact with a substrate for a long period of time, the enzyme gradually acts on the substrate, for which reason the reagent containing the enzyme and a substrate need to be used immediately for the determination of .alpha. (justia.com)
- This method is advantageous in that the substrate is not attacked by an adjuvant enzyme before the action of .alpha. (justia.com)
- Accordingly, reagents are still usable upon long-term storage after preparation of reagents containing the enzyme and the substrate, enabling preparation of a single-vial reagent containing enzyme(s) and substrate(s) for the determination of .alpha. (justia.com)
- A genetic deficiency or lysosomal enzyme acid alpha-glucosidase (GAA) dysfunction causes Pompe disease. (pharmaceutical-technology.com)
- Pompe disease is a genetic disease that occurs when a specific enzyme (acid alpha-glucosidase) is absent or the body doesn't produce enough. (dukehealth.org)
- These tests look for the presence of a key enzyme -- acid alpha-glucosidase - as well as the buildup of glycogen in muscle and tissues in the body. (dukehealth.org)
Glycogen3
- Lysosomal Alpha Glucosidase (GAA, otherwise called Alpha Acid-Glucosidase) is a catalyst that corrupts glycogen into glucose. (phrconference.org)
- Mutations in the GAA gene prevent acid alpha-glucosidase from breaking down glycogen effectively, which allows this sugar to build up to toxic levels in lysosomes. (nih.gov)
- Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II . (nih.gov)
Deficiency1
- Fukuda T, Roberts A, Plotz PH, Raben N. Acid alpha-glucosidase deficiency (Pompe disease). (nih.gov)
Acarbose3
- Among all the tested compounds, 102 & 105 has displayed the most potent activity against a -glucosidase with the IC 50 of 142.21±1.8 mM and 182.83±2.43 mM respectively, as compared to the standard drug acarbose (136.89±1.67 mM). (thesciencein.org)
- Results showed that grape seed extract strongly inhibited both α-amylase and α-glucosidase activity, with equal and much higher potency, respectively, than acarbose. (nih.gov)
- Acarbose Tablets are an oral alpha-glucosidase inhibitor for use in the management of type 2 diabetes mellitus. (nih.gov)
Intestinal1
- Pancreatic alpha-amylase hydrolyzes complex starches to oligosaccharides in the lumen of the small intestine, while the membrane-bound intestinal alpha-glucosidases hydrolyze oligosaccharides, trisaccharides, and disaccharides to glucose and other monosaccharides in the brush border of the small intestine. (nih.gov)
Lysosomal1
- ELISA Kit for the in vitro quantitative estimation of Human Lysosomal Alpha Glucosidase (GAA) focuses in tissue homogenates, cell lysates and other natural liquids. (phrconference.org)
Glucose7
- Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. (nih.gov)
- amylase substrate and optically determining a liberated label, the substrate being a maltooligosaccharide composed of at least 3 glucose units, whose reducing terminal glucose is bonded to an optically measurable label at the 1-position by .alpha. (justia.com)
- glucoside linkage, and whose non-reducing terminal glucose is modified by a substituent other than glucose, and the .alpha. (justia.com)
- glucosidase being substantially capable of acting on glucose to which the label is bonded at the 1-position by .alpha. (justia.com)
- Amylase activity has hitherto been determined by using a maltooligosaccharide having an unmodified non-reducing terminal glucose and .alpha. (justia.com)
- glucosidase also acts on maltooligosaccharides whose reducing terminal glucose is bonded to a label, but scarcely acts on maltooligosaccharides having a glucose chain length equal to or longer than that of maltotetraose (G4), it acts very slowly on maltooligosaccharides having a chain length not less than G4 and unmodified non-reducing terminal glucose prior to the action of .alpha. (justia.com)
- glucosidase originated from yeast, however, exhibits lowered activity as the glucose chain becomes longer. (justia.com)
Pancreatic1
- amylase activity in body fluid, which is a clinical parameter in the diagnoses of pancreatic diseases and sialadenotropic diseases, and to reagents for the determination of .alpha. (justia.com)
Activity2
- amylase activity which involves bringing a sample into contact with an .alpha. (justia.com)
- amylase activity comprising the .alpha. (justia.com)
Presence1
- glucosidase in the presence of an .alpha. (justia.com)
Analysis1
- Comparative analysis among fully sequenced Dyella species indicate that the genome synteny is not conserved, and that D. jiangningensis FCAV SCS01 carries 372 unique genes, including an alpha-glucosidase and maltodextrin glucosidase coding genes, and other potential biomass degradation related genes. (mendeley.com)
Beta1
- glucosidase and, if necessary, .beta. (justia.com)
Method5
- US Patent for Method for determination of .alpha. (justia.com)
- Method for determination of .alpha. (justia.com)
- A method for determining .alpha. (justia.com)
- The present invention relates to a method for the determination of .alpha. (justia.com)
- Nonetheless, this method also poses problems of specificity of .alpha. (justia.com)
Structure1
- Novel Catalytic Mechanism of Glycoside Hydrolysis Based on the Structure of an NAD(+)/Mn(2+)-Dependent Phospho-alpha-Glucosidase from Bacillus subtilis. (expasy.org)
Sensitive1
- glucosidase for a substrate, and for a sensitive determination to be conducted by an efficient adjuvant reaction, it is required to add a large excess of .alpha. (justia.com)
Lysosomal2
Acid3
- Many of these mutations change one of the protein building blocks (amino acids) used to make acid alpha-glucosidase. (nih.gov)
- Fukuda T, Roberts A, Plotz PH, Raben N. Acid alpha-glucosidase deficiency (Pompe disease). (nih.gov)
- Yan B, Raben N, Plotz P. The human acid alpha-glucosidase gene is a novel target of the Notch-1/Hes-1 signaling pathway. (nih.gov)
Catechins2
- This study evaluated the inhibitory effects of plant-based extracts (grape seed, green tea, and white tea) and their constituent flavan-3-ol monomers (catechins) on α-amylase and α-glucosidase activity, two key glucosidases required for starch digestion in humans. (nih.gov)
- 1. alpha-Glucosidase inhibitory profile of catechins and theaflavins. (nih.gov)
Gene1
- Genomic organization and promoter activity of glucosidase I gene. (nih.gov)