alpha-L-Fucosidase: An enzyme that catalyzes the hydrolysis of an alpha L-fucoside to yield an alcohol and L-fucose. Deficiency of this enzyme can cause FUCOSIDOSIS. EC 3.2.1.51.FucoseFucosidosis: An autosomal recessive lysosomal storage disease caused by a deficiency of ALPHA-L-FUCOSIDASE activity resulting in an accumulation of fucose containing SPHINGOLIPIDS; GLYCOPROTEINS, and mucopolysaccharides (GLYCOSAMINOGLYCANS) in lysosomes. The infantile form (type I) features psychomotor deterioration, MUSCLE SPASTICITY, coarse facial features, growth retardation, skeletal abnormalities, visceromegaly, SEIZURES, recurrent infections, and MACROGLOSSIA, with death occurring in the first decade of life. Juvenile fucosidosis (type II) is the more common variant and features a slowly progressive decline in neurologic function and angiokeratoma corporis diffusum. Type II survival may be through the fourth decade of life. (From Menkes, Textbook of Child Neurology, 5th ed, p87; Am J Med Genet 1991 Jan;38(1):111-31)Lymphocyte Function-Associated Antigen-1: An integrin heterodimer widely expressed on cells of hematopoietic origin. CD11A ANTIGEN comprises the alpha chain and the CD18 antigen (ANTIGENS, CD18) the beta chain. Lymphocyte function-associated antigen-1 is a major receptor of T-CELLS; B-CELLS; and GRANULOCYTES. It mediates the leukocyte adhesion reactions underlying cytolytic conjugate formation, helper T-cell interactions, and antibody-dependent killing by NATURAL KILLER CELLS and granulocytes. Intracellular adhesion molecule-1 has been defined as a ligand for lymphocyte function-associated antigen-1.Glycoside HydrolasesAntigens, CD18: Cell-surface glycoprotein beta-chains that are non-covalently linked to specific alpha-chains of the CD11 family of leukocyte-adhesion molecules (RECEPTORS, LEUKOCYTE-ADHESION). A defect in the gene encoding CD18 causes LEUKOCYTE-ADHESION DEFICIENCY SYNDROME.Integrins: A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors(RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation.Integrin alpha4beta1: Integrin alpha4beta1 is a FIBRONECTIN and VCAM-1 receptor present on LYMPHOCYTES; MONOCYTES; EOSINOPHILS; NK CELLS and thymocytes. It is involved in both cell-cell and cell- EXTRACELLULAR MATRIX adhesion and plays a role in INFLAMMATION, hematopoietic cell homing and immune function, and has been implicated in skeletal MYOGENESIS; NEURAL CREST migration and proliferation, lymphocyte maturation and morphogenesis of the PLACENTA and HEART.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Cell Adhesion: Adherence of cells to surfaces or to other cells.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.alpha 1-Antitrypsin: Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.Fluorescent Dyes: Agents that emit light after excitation by light. The wave length of the emitted light is usually longer than that of the incident light. Fluorochromes are substances that cause fluorescence in other substances, i.e., dyes used to mark or label other compounds with fluorescent tags.DisaccharidasesOctopodiformes: A superorder in the class CEPHALOPODA, consisting of the orders Octopoda (octopus) with over 200 species and Vampyromorpha with a single species. The latter is a phylogenetic relic but holds the key to the origins of Octopoda.Isoelectric Focusing: Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Methylmalonate-Semialdehyde Dehydrogenase (Acylating): An enzyme that plays a role in the VALINE; LEUCINE; and ISOLEUCINE catabolic pathways by catalyzing the oxidation of 2-methyl-3-oxopropanate to propanoyl-CoA using NAD+ as a coenzyme. Methylmalonate semialdehyde dehydrogenase deficiency is characterized by elevated BETA-ALANINE and 3-hydropropionic acid.Kinetics: The rate dynamics in chemical or physical systems.MedlinePlus: NATIONAL LIBRARY OF MEDICINE service for health professionals and consumers. It links extensive information from the National Institutes of Health and other reviewed sources of information on specific diseases and conditions.Glycolipids: Any compound containing one or more monosaccharide residues bound by a glycosidic linkage to a hydrophobic moiety such as an acylglycerol (see GLYCERIDES), a sphingoid, a ceramide (CERAMIDES) (N-acylsphingoid) or a prenyl phosphate. (From IUPAC's webpage)Carbohydrate Metabolism, Inborn ErrorsHydrothermal Vents: Hot springs on the ocean floor. They are commonly found near volcanically active places such as mid-oceanic ridges.FuraldehydeSearch Engine: Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.Databases, Genetic: Databases devoted to knowledge about specific genes and gene products.RNA Folding: The processes of RNA tertiary structure formation.Streptococcus pneumoniae: A gram-positive organism found in the upper respiratory tract, inflammatory exudates, and various body fluids of normal and/or diseased humans and, rarely, domestic animals.Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase: A group of related enzymes responsible for the endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose-content glycopeptides and GLYCOPROTEINS.Hexosaminidase A: A mammalian beta-hexosaminidase isoform that is a heteromeric protein comprized of both hexosaminidase alpha and hexosaminidase beta subunits. Deficiency of hexosaminidase A due to mutations in the gene encoding the hexosaminidase alpha subunit is a case of TAY-SACHS DISEASE. Deficiency of hexosaminidase A and HEXOSAMINIDASE B due to mutations in the gene encoding the hexosaminidase beta subunit is a case of SANDHOFF DISEASE.Serotyping: Process of determining and distinguishing species of bacteria or viruses based on antigens they share.alpha-Mannosidase: An enzyme that catalyzes the HYDROLYSIS of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides. The enzyme plays a role in the processing of newly formed N-glycans and in degradation of mature GLYCOPROTEINS. There are multiple isoforms of alpha-mannosidase, each having its own specific cellular location and pH optimum. Defects in the lysosomal form of the enzyme results in a buildup of mannoside intermediate metabolites and the disease ALPHA-MANNOSIDOSIS.Hexosaminidases: Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.Endotoxins: Toxins closely associated with the living cytoplasm or cell wall of certain microorganisms, which do not readily diffuse into the culture medium, but are released upon lysis of the cells.Limulus Test: Sensitive method for detection of bacterial endotoxins and endotoxin-like substances that depends on the in vitro gelation of Limulus amebocyte lysate (LAL), prepared from the circulating blood (amebocytes) of the horseshoe crab, by the endotoxin or related compound. Used for detection of endotoxin in body fluids and parenteral pharmaceuticals.Pacific OceanAlkaline Ceramidase: A ceramidase subtype that is active at alkaline pH. It is found at high levels within the SMALL INTESTINE.Neutral Ceramidase: A ceramidase subtype that is active at neutral pH. It is found at high levels within the SMALL INTESTINE and in the BRAIN.Acid Ceramidase: A ceramidase subtype that is active at acid pH. It plays an important role in sphingolipid degradation by catalyzing the lysosomal hydrolysis of ceramide to sphingosine and free fatty acid. Inherited deficiency of acid ceramidase activity results in FARBER LIPOGRANULOMATOSIS.Serine C-Palmitoyltransferase: A key enzyme in SPHINGOLIPIDS biosynthesis, this enzyme catalyzes the pyridoxal-5'-phosphate-dependent condensation of L-SERINE and PALMITOYL COENZYME A to 3-dehydro-D-sphinganine. The enzyme consists of two different subunits.Ceramidases: Amidohydrolases that are specific for the cleavage of the N-acyl linkage of CERAMIDES. Ceramidases are classified as acidic, neutral or basic according to the optimal pH with which they function.Horses: Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest.Acer: A plant genus of the family ACERACEAE, best known for trees with palmately lobed leaves.Copyright: It is a form of protection provided by law. In the United States this protection is granted to authors of original works of authorship, including literary, dramatic, musical, artistic, and certain other intellectual works. This protection is available to both published and unpublished works. (from Circular of the United States Copyright Office, 6/30/2008)Charities: Social welfare organizations with programs designed to assist individuals in need.Zebrafish: An exotic species of the family CYPRINIDAE, originally from Asia, that has been introduced in North America. They are used in embryological studies and to study the effects of certain chemicals on development.Zebrafish Proteins: Proteins obtained from the ZEBRAFISH. Many of the proteins in this species have been the subject of studies involving basic embryological development (EMBRYOLOGY).Slavery: The status or condition of a person over whom any or all of the powers attaching to the right of ownership are exercised. The slave trade is all acts involved in the capture, acquisition or disposal of persons with intent to reduce them to enslavement; all acts involved in the acquisition of enslaved persons with a view to selling or exchanging them; all acts of disposal by sale or exchange of persons acquired with a view to being sold or exchanged, and, in general, every act of trade or transport of slaves. ( from http://www.ohchr.org/Documents/Publications/slaveryen.pdf accessed 10/18/2012)National Human Genome Research Institute (U.S.): Component of the NATIONAL INSTITUTES OF HEALTH. It conducts and supports research into the mapping of the human genome and other organism genomes. The National Center for Human Genome Research was established in 1989 and re-named the National Human Genome Research Institute in 1997.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

Endometrial lysosomal enzyme activity in normal cycling endometrium. (1/168)

The objective of this study was to evaluate the possible role of four lysosomal enzymes in endometrial function and remodelling during the normal menstrual cycle by fluorimetric measurement (acid phosphatase, N-acetyl-beta-D-glucosaminidase, alpha-L-fucosidase and alpha-D-mannosidase). A prospective study was conducted of 45 endometrial biopsies obtained from women with normal menstrual cycles. Activity of all four enzymes was identified in human endometrium. Activity of acid phosphatase and N-acetyl-beta-D-glucosaminidase was relatively high, whilst that of alpha-L-fucosidase and alpha-D-mannosidase was low. There was no significant change in the activity of any of the four enzymes from the proliferative to the secretory phase of the cycle. This study suggests that the activity of these enzymes remains constant throughout a major portion of the normal cycle.  (+info)

Characterization of human semen alpha-L-fucosidases. (2/168)

Human semen contains a large amount of alpha-L-fucosidase activity, the great majority of which is found in the seminal fluid. Immunocytochemical studies indicate that a small amount of semen fucosidase activity is present on the sperm plasma membrane, primarily in the posterior head region. Subcellular fractionation studies also indicate that sperm alpha-L-fucosidase is present in the plasma membrane-enriched fraction. Comparative characterization of human seminal fluid and sperm alpha-L-fucosidases indicates that seminal fluid alpha-L-fucosidase has a broad pH optimum curve with a number of near-equal maxima between pH 4.8 and 7.0 while sperm fucosidase has a major optimum between pH 3.4 and 4.0. Isoelectric focusing indicates that seminal fluid alpha-L-fucosidase contains three to six isoforms with isoelectric points (pI) of 5-7 while sperm fucosidase contains two distinct isoforms with pI values of 5. 2 +/- 0.2 and 7.0 +/- 0.2. Western blotting indicates that seminal fluid fucosidase contains a major protein band with a molecular mass ratio (M(r)) of approximately 56 kDa while sperm fucosidase contains a major protein band of approximately 51 kDa. The overall results indicate the presence of a low-abundance, plasma membrane-associated human sperm alpha-L-fucosidase, which is different in its properties from human seminal fluid alpha-L-fucosidase(s), and whose function is not yet known.  (+info)

Fucose in alpha(1-6)-linkage regulates proliferation and histogenesis in reaggregated retinal spheroids of the chick embryo. (3/168)

We have used the lectin from Aleuria aurantia (AAL) which is highly specific for alpha(1-6)-linked fucose, to examine its effect on chicken retinogenesis in a reaggregation culture system. When dispersed cells of the embryonic chick retina are reaggregated to form histotypic retinospheroids, AAL elicits strong inhibition of spheroid growth. The action of AAL is specific, since its effect is dose-dependent, saturable, and inhibited by an excess of fucose. Fucosidase treatment entirely abolishes reaggregation. In contrast, Anguilla anguilla agglutinin (AAA) binding to fucose in alpha(1-2)-linkage does not show any effects. Incubation with CAB4-a specific monoclonal antibody for fucose in alpha(1-6)-linkage-reduces spheroid size and shape. AAL does not much affect primary aggregation, but rather subsequent processes of cell proliferation and histogenesis. In particular, AAL inhibits uptake of bromo-desoxyuridine (BrdU), most efficiently so during days in vitro 2 (div2) and div3. As a consequence, the histological differentiation is entirely disturbed, as evidenced by vimentin immunostaining; particularly, rosettes are not forming and the radial glia scaffold is disorganized. We conclude that glycoproteins exhibiting fucose in alpha(1-6)-linkage may play major roles in early processes of retinal tissue formation.  (+info)

Glycosylation alterations of cells in late phase apoptosis from colon carcinomas. (4/168)

Comparisons of carbohydrate profiles between control and apoptotic colon carcinoma cells were performed by flow cytometry using a set of lectins and anti-carbohydrate antibodies. The six cell lines analyzed presented distinct carbohydrate profiles before induction of apoptosis. PHA-L and MAA binding decreased after induction of apoptosis by UV-treatment. In contrast an increase of PNA binding was observed after induction of apoptosis, except on SW-48 cells for which a decrease occurred. A decrease of SNA binding was observed after induction of apoptosis from strongly positive control cell lines, whereas it increased on weakly positive ones. All the blood group related antigens A, H, Lewis a, Lewis x, Lewis b, and Lewis y, had their expression strongly diminished on apoptotic cells. These changes occurred irrespective of the mode of apoptosis induction since similar results were obtained after UV, TNFalpha, or anti-Fas treatment. Fucosyltransferases activities were also decreased after apoptosis induction, except for alpha1,3fucosyltransferase in anti-Fas treated HT-29 cells, where it was strongly augmented. This could be attributed to the IFNgamma preteatment required to induce Fas expression on these cells. Fucosidase activity decreased after induction of apoptosis suggesting that it was not responsible for the loss of fucosylated structures. In the rat PRO cell line, H blood group antigens are mainly carried by a high molecular weight variant of CD44. It could be shown that the loss of H antigen after induction of apoptosis correlated with a loss of the carrier glycoprotein.  (+info)

Terminal glycosylation in cystic fibrosis. (5/168)

Cystic fibrosis (CF) is a common genetic disease for which the gene was identified within the last decade. Pulmonary disease predominates in this ultimately fatal disease and current therapy only slows the progression. CF transmembrane regulator (CFTR), the gene product, is an integral membrane glycoprotein that normally functions as a chloride channel in epithelial cells. The most common mutation, deltaF508, results in mislocalization and altered glycosylation of CFTR. Altered fucosylation and sialylation are hallmarks of both membrane and secreted glycoproteins in CF and the focus here is on these investigations. Oligosaccharides from CF membrane glycoproteins have the Lewis x, selectin ligand in terminal positions. In addition, two major bacterial pathogens in CF, Pseudomonas aeruginosa and Haemophilus influenzae, have binding proteins, which recognize fucose in alpha1,3 linkage and asialoglycoconjugates. We speculate that the altered terminal glycosylation of airway epithelial glycoproteins in CF contributes to the chronic infection and robust inflammatory response in the CF lung. Understanding the effects of mutant CFTR on glycosylation may provide further insight into the regulation of glycoconjugate processing as well as therapy for CF.  (+info)

Prediction of the development of hepato-cellular-carcinoma in patients with liver cirrhosis by the serial determinations of serum alpha-L-fucosidase activity. (6/168)

OBJECTIVE: Evaluation of the usefulness of the serial determinations of serum alpha-L-fucosidase (AFU) activity for prediction of the development of hepatocellular carcinoma (HCC) was performed. METHODS AND PATIENTS: Serum AFU activity was determined monthly for 42 months in 73 patients with liver cirrhosis (LC). RESULTS: HCC was diagnosed in 27 patients by means of ultrasonography during this observation period. In 23 (85%) of the 27 patients, serum AFU activity was found to exceed 700 nmole/ml/h during the LC stage. HCC developed within a few years in 23 (82%) of 28 LC patients with AFU activity exceeding 700 nmole/ml/h, in contrast, it developed in only 4 (9%) of 45 LC patients with AFU activity below 700 nmole/ml/h. AFU activity was already elevated in 23 (85%) of 27 patients at least 6 months before the detection of HCC by ultrasonography. CONCLUSION: It is conceivable that the development of HCC can be predicted by means of serial determinations of serum AFU activity in patients with LC.  (+info)

Endometrial lysosomal enzyme activity in ovulatory dysfunctional uterine bleeding, IUCD users and post-partum women. (7/168)

The aim of this study was to evaluate the role of lysosomal enzymes in excessively heavy menstruation by comparing women with menorrhagia due to dysfunctional bleeding or intrauterine contraceptive device (IUCD) use with those with normal menstrual periods or with amenorrhoea associated with breastfeeding. This was a prospective cohort investigation of the activity of four endometrial lysosomal enzymes in three contrasting groups: (i) women with ovulatory dysfunctional uterine bleeding and users of intrauterine contraceptive devices; (ii) breastfeeding post-partum women in whom there are long periods of amenorrhoea, particularly in the early months post-partum; and (iii) normal cycling women. It was found that the total activity of lysosomal enzymes, particularly acid phosphatase and N-acetyl-beta-D-glucosaminidase, was markedly elevated (P < 0.001) in IUCD-exposed endometrium, and endometrium from women with dysfunctional uterine bleeding when compared with endometrium from women with a history of entirely normal menstrual periods or that in post-partum breastfeeding women. The activity of alpha-L-fucosidase was moderately elevated in IUCD users (P < 0.05) and ovulatory dysfunctional uterine bleeding (P < 0.05), whereas alphaD-mannosidase activity was elevated in ovulatory dysfunctional uterine bleeding (P < 0.05), but decreased in IUCD users (P < 0.01). No significant differences were observed in the lysosomal enzyme activities of breastfeeding post-partum women and normal cycling women. These results show that total endometrial tissue activity of four lysosomal enzymes was substantially increased throughout the cycle in most circumstances in women with two different causes for increased menstrual bleeding. This suggests a contributory role to the increased bleeding.  (+info)

Sequence and expression of Thai Rosewood beta-glucosidase/beta-fucosidase, a family 1 glycosyl hydrolase glycoprotein. (8/168)

Dalcochinin-8'-O-beta-glucoside beta-glucosidase (dalcochinase) from the Thai rosewood (Dalbergia cochinchinensis Pierre) has aglycone specificity for isoflavonoids and can hydrolyze both beta-glucosides and beta-fucosides. To determine its structure and evolutionary lineage, the sequence of the enzyme was determined by peptide sequencing followed by PCR cloning. The cDNA included a reading frame coding for 547 amino acids including a 23 amino acid propeptide and a 524 amino acid mature protein. The sequences determined at peptide level were found in the cDNA sequence, indicating the sequence obtained was indeed the dalcochinase enzyme. The mature enzyme is 60% identical to the cyanogenic beta-glucosidase from white clover glycosyl hydrolase family 1, for which an X-ray crystal structure has been solved. Based on this homology, residues which may contribute to the different substrate specificities of the two enzymes were identified. Eight putative glycosylation sites were identified, and one was confirmed to be glycosylated by Edman degradation and mass spectrometry. The protein was expressed as a prepro-alpha-mating factor fusion in Pichia pastoris, and the activity of the secreted enzyme was characterized. The recombinant enzyme and the enzyme purified from seeds showed the same K(m) for pNP-glucoside and pNP-fucoside, had the same ratio of V(max) for these substrates, and similarly hydrolyzed the natural substrate, dalcochinin-8'-beta-glucoside.  (+info)

Définitions de 1 3 alpha l fucosidase, synonymes, antonymes, dérivés de 1 3 alpha l fucosidase, dictionnaire analogique de 1 3 alpha l fucosidase (anglais)
Alpha-l-fucosidase (AFU) plays vital roles in some physiological processes that closely relate to several diseases. Herein, a ratiometric fluorescent probe for the alpha-l-fucosidase (AFU) assay based on a single fluorophore has been developed by functionalizing a new fluorophore platform (6-bromo-anthracene MCF Editors Recommendation
While the catalytic nucleophile in the configuration-retaining alpha-L-fucosidases from family GH29 is fully conserved with respect to sequence, there is no fully sequence-conserved acid/base residue candidate across the family. X-ray crystallographic studies and kinetic characterizations have allowed the identification of this residue in a few cases, and a recent combination of phylogenetic tree analyses with substrate specificity data has allowed the division of GH29 enzymes into two subfamilies, A and B, allowing the probable assignment of these residues. Here, we perform detailed kinetic and mechanistic characterizations of the corresponding alanine mutants and other candidates. Through comparison of kinetic parameters obtained for the hydrolysis of fucosyl substrates with activated leaving groups by these mutants with those of the corresponding wild-type enzymes, in conjunction with the demonstration of azide rescue, we largely confirm the acid/base residue predictions for the GH29 ...
BioAssay record AID 36841 submitted by ChEMBL: Inhibition of the enzyme alpha-L-fucosidase from bovine epididymis was determined at 1 mM concentration of the compound; No inhibition.
K01186 NEU1; sialidase-1 [EC:3.2.1.18] K01186 NEU1; sialidase-1 [EC:3.2.1.18] K01190 lacZ; beta-galactosidase [EC:3.2.1.23] K12373 HEXA_B; hexosaminidase [EC:3.2.1.52] K12373 HEXA_B; hexosaminidase [EC:3.2.1.52] K01191 MAN2C1; alpha-mannosidase [EC:3.2.1.24] K01227 E3.2.1.96; mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [EC:3.2.1.96] K01206 FUCA; alpha-L-fucosidase [EC:3.2.1.51] K15923 AXY8; alpha-L-fucosidase 2 [EC:3.2.1.51 ...
Glycosylation drives critical processes important for mammalian cell-cell and cell-matrix interactions. Alpha-l-fucose (α-l-f) is a key monosaccharide component of oligosaccharides that has been found to be overexpressed during tumor progression. Modification of cell surface fucosylation, we hypothesized, alters tumor cell phenotype and function at the end of the neoplastic progression cascade including tumor invasion. Alpha-l-fucosidase (α-l-fase) is a glycosidase that specifically removes (α-l-f) from oligosaccharide sites. We first verified the effectiveness of the α-l-fase to specifically decrease the level of α-l-f on the cell surface of several human breast cancer cell lines and also examined the recovery time for these cells to repopulate their surfaces. To investigate the potential effect of defucosylation on tumor functions, we studied the proliferation, and invasion in vitro of human breast cancer MDA-MB-231 cells as the representative cell model. We further examined several ...
Math o ganser syn cychwyn yn yr afu yw canser yr afu, a elwir hefyd yn ganser hepatig a chanser hepatig cynradd.[1] Mae canserau sydd wedi lledaeni ir afu o lefydd eraill yn y corff (metastasis yr afu) llawer mwy cyffredin na chyflyrau syn cychwyn yn yr afu.[2] Gall canser yr afu achosi symptomau megis ymdeimlad o boen neu lwmp gweledol islawr gawell asennau ar yr ochr dde, chwyddo yn yr abdomen, croen melyn, cleisio hawdd, colli pwysau a gwendid cyffredinol. Achosir y rhan fwyaf o gyflyrau canser yr afu gan sirosis o ganlyniad i hepatitis B, hepatitis C, neu alcohol.[3] Ymhlith yr achosion eraill y mae afflatocsin, afiechyd afu brasterog di-alcohol, a llyngyr yr afu. Y mathau mwyaf cyffredin or cyflwr yw carsinoma hepatogellol neu HCC (80% o achosion), a cholangiocarcinoma. Ceir rhai llai cyffredin yn ogystal, er enghraifft neoplasm systig mwsinog a neoplasm bustlaidd papilaidd anhydradwyol. Gellir cadarnhau diagnosis drwy brawf gwaed a delweddu meddygol a chanfod tystiolaeth bellach or ...
Complete information for FUCA1P1 gene (Pseudogene), Alpha-L-Fucosidase 1 Pseudogene 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
... - Instruments Consumables Reagents Advanced BioMatrix,RANDOX,RANDOX ELISA,Biomedical, biochemical reagents, laboratory supplies, equipment, antibodies, ELISA kits, diagnostic reagents, methods of experimental techniques, general analytical instruments, material testing instruments and equipment, used laboratory equipment, instruments and equipment, life sciences, environmental monitoring equipment , measurement, measuring instruments, rotating wall bioreactor, three-dimensional tissue / stem cell culture system; microcapsule
A series of phenyl-D-thioglucopyranosides were prepared and characterized in order to determine the absolute specificity of the .B-thioglucosidase and B-glucosidese enzyme systems toward the th1oglucosidic bond. The specificity of B-glucosidase of almond emulsin toward oxygen linkage seems to be absolute, since no hydrolysis was observed by this enzyme system toward the phenyl-D-thioglucopyranosides. The P-th1oglucosidase system was found to hydrolyze only two of the thioglucopyranosides. It was apparent that only where the electron-attracting substituents in the phenyl group were strong enough to greatly weaken the strength of the sulfur linkage, as in the case of the nitro group, would there be any hydrolysis. The lack of hydrolysis prevented application of the Hammett equation in testing the quantitative electronic effects of the substitutents on the rate of bond hydrolysis.
Complete information for FUCA1 gene (Protein Coding), Fucosidase, Alpha-L- 1, Tissue, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
The chemical relationship of the seven forms of human liver α-L fucosidase has been studied by isoelectric focusing of neuraminidase- and sialyltransf
endo-β-1,4-xylanase (EC 3.2.1.8); β-glucosidase (3.2.1.21); β-glucuronidase (EC 3.2.1.31); β-xylosidase (EC 3.2.1.37); β-fucosidase (EC 3.2.1.38); glucosylceramidase (EC 3.2.1.45); β-1,6-glucanase (EC 3.2.1.75); glucuronoarabinoxylan endo-β-1,4-xylanase (EC 3.2.1.136); endo-β-1,6-galactanase (EC:3.2.1.164); [reducing end] β-xylosidase (EC 3.2.1.- ...
endo-β-1,4-xylanase (EC 3.2.1.8); β-glucosidase (3.2.1.21); β-glucuronidase (EC 3.2.1.31); β-xylosidase (EC 3.2.1.37); β-fucosidase (EC 3.2.1.38); glucosylceramidase (EC 3.2.1.45); β-1,6-glucanase (EC 3.2.1.75); glucuronoarabinoxylan endo-β-1,4-xylanase (EC 3.2.1.136); endo-β-1,6-galactanase (EC:3.2.1.164); [reducing end] β-xylosidase (EC 3.2.1.- ...
Fast delivery of FUCA2 knockout Human Cell Lines for the study of gene function. Created by CRISPR/Cas9 genome editing. Includes matched wildtype control.
chains in the Genus database with same CATH superfamily 4XNL A; 4AZL A; 4AFK A; 5D5D A; 4B61 A; 5IYU A; 3RBH A; 4XNK A; #chains in the Genus database with same CATH topology 2R4O A; 1GFM A; 1YS5 A; 1T16 A; 2XTQ A; 3G7G A; 3LK3 B; 2Y0L A; 1H6S 1; 4FRX A; 5KAF O; 4FQE A; 3TZG A; 5AFU K; 3POX A; 4RL9 A; 1P4T A; 2F1T A; 4U9C A; 2X27 X; 3AA6 A; 2W81 C; 3SYS A; 5GV0 A; 3V8U A; 5DL5 A; 4AYI D; 3WI4 A; 3SZV A; 1BH3 A; 2M07 A; 4FZM A; 3PGU A; 3VE1 A; 4C00 A; 3T24 A; 4GHB A; 5JDP A; 4O3Z A; 2XMX A; 3BRY A; 4D5U A; 4AKR B; 2M06 A; 3A2S X; 4GF4 A; 2KZ7 B; 3DA3 A; 3POQ A; 4FSP A; 2AXT O; 3HOE A; 5FVN A; 3DWN A; 3PF1 A; 3RBH A; 3AA0 B; 4LSE A; 2F1V A; 2XG6 A; 2X9K A; 1Q9F A; 4PR7 A; 4B61 A; 3HW9 A; 4O3W A; 5G39 A; 4JCH A; 2MHL A; 5AFU L; 2W80 C; 2R4P A; 1QJ9 A; 3POR A; 5IYU A; 2KXP B; 1ORM A; 4KR8 A; 4K3C A; 1IZN A; 4O4U A; 5D5D A; 3PRN A; 4AYD C; 4KR4 A; 3VZW X; 5DL7 A; 1GFO A; 3BS0 A; 3LK4 1; 2N2L A; 3NSG A; 4G75 A; 4JFB A; 4LSI A; 4O4X A; 4RLC A; 3T0S A; 3AA7 B; 2KZ7 A; 3VZU X; 4D64 A; 2R4N A; 4AKR A; 3PQU ...
The molecular basis of the deficiency of alpha-L-fucosidase has been investigated in eight patients who had been diagnosed clinically and enzymatically as suffering from the autosomal recessive lysosomal storage disease fucosidosis. None of the patients had a deletion or gross alteration of the alpha-L-fucosidase gene (FUCA1). Single strand conformation polymorphism (SSCP) analysis followed by direct sequencing of amplified exons and flanking regions identified putative disease causing mutations in six of the patients, who had severe forms of the disease and very low residual alpha-L-fucosidase activity and protein. They were a 10 bp deletion in exon 1 (E113fs), a 1 bp deletion at position -2 of intron 2 (S216fs), a g--,a transition at IVS5+1, point mutations W183X and N329Y in exons 3 and 6, respectively, and a compound allele consisting of a point mutation in the signal peptide in exon 1, P5R, and a 1 bp insertion in exon 6 (Y330fs). One patient in whom an SSCP change was not detected had ...
Fucosidosis is a rare lysosomal storage disorder caused by the inherited deficiency of the lysosomal hydrolase α-L-fucosidase, which leads to an impaired degradation of fucosylated glycoconjugates. Here we report the generation of a fucosidosis mouse model, in which the gene for lysosomal α-L-fucosidase (Fuca1) was disrupted by gene targeting. Homozygous knock-out mice completely lack α-L-fucosidase activity in all tested organs leading to highly elevated amounts of the core-fucosylated glycoasparagine Fuc(α1,6)-GlcNAc(β1-N)-Asn and, to a lesser extent, other fucosylated glycoasparagines, which all were also partially excreted with the urine. Lysosomal storage pathology was observed in many visceral organs like liver, kidney, spleen and bladder as well as in the CNS. On the cellular level storage was characterized by membrane-limited cytoplasmic vacuoles primarily containing water-soluble storage material. In the CNS cellular alterations included enlargement of the lysosomal compartment in ...
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InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
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Recombinant Human FUCA1 protein is an Insect Full length protein 28 to 466 aa range, | 90% purity, | 1.000 Eu/µg endotoxin level and validated in SDS-PAGE.
Expression of FUCA2 (dJ20N2.5, MGC1314) in caudate tissue. Antibody staining with HPA031659, HPA031660 and HPA031661 in immunohistochemistry.
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At least 26 mutations in the FUCA1 gene have been found to cause fucosidosis. Most of these mutations result in an abnormally short, nonfunctional alpha-L-fucosidase enzyme. Without this enzyme, glycolipids and glycoproteins cannot be completely broken down. These partially broken down compounds accumulate in the lysosomes and cause cells throughout the body to malfunction. Brain cells are particularly sensitive to the buildup of glycolipids and glycoproteins, which can result in cell death. Loss of brain cells is thought to cause the neurological symptoms of fucosidosis. Accumulation of glycolipids and glycoproteins also occurs in other organs such as the liver, spleen, skin, heart, pancreas, and kidneys, contributing to the additional symptoms of fucosidosis. ...
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Background: Some salivary markers of alcohol abuse/dependence have been proposed so far: aminotransferases, gamma-glutamyltransferase, ethanol, ethyl glucuronide, ethyl sulfate, sialic acid, β-hexosaminidase A, oral peroxidase, methanol, diethylene/ethylene glycol, α-amylase, clusterin, haptoglobin, heavy/light chains of immunoglobulins and transferrin. Aim: To investigate the effect of chronic alcohol drinking and smoking on the activity (pKat/ml) and output (pKat/min) of salivary lysosomal exoglycosidases: α-fucosidase (FUC), α-mannosidase (MAN), β-galactosidase (GAL), and β-glucuronidase (GLU), and their applicability as markers of alcohol dependence. Methods: The activity of FUC, MAN, GAL and GLU was measured colorimetrically in the saliva of healthy social drinkers, alcohol-dependent non-smokers and alcohol-dependent smokers. Results: We observed an increased salivary activity of FUC, GAL, GLU and MAN, as well as an increased output of GAL and GLU, in comparison with controls. The ...
Catheter ablation of atrial fibrillation (AFCA) efficacy in patients with impaired left ventricular systolic function improves when performed early in the natural history of atrial fibrillation (AF) and heart failure, according to a study published recently in Circulation: Arrhythmia and Electrophysiology.1 AFCA provides long-term benefits on left ventricular function, significantly reducing the number of patients with severely impaired systolic function, the authors add. ...
Expression of FUCA2 (dJ20N2.5, MGC1314) in pancreas tissue. Antibody staining with HPA031659, HPA031660 and HPA031661 in immunohistochemistry.
chains in the Genus database with same CATH superfamily 3M0U A; 2DX1 A; 2KR3 A; 1JO8 A; 1BU1 A; 2KRM A; 2NWM A; 1OV3 A; 1X6B A; 3PVL A; 1PKS A; 1M8M A; 2A08 A; 2EQI A; 3EG3 A; 2ED1 A; 5FWC A; 2O9S A; 2O2O A; 2KYB A; 4E6R A; 1QCF A; 2MCN A; 3FJ5 A; 2LX7 A; 4M4Z A; 2M0Y A; 2MOX A; 3VS2 A; 1HD3 A; 4R0K A; 1W1F A; 3H0H A; 2JXB A; 1GL5 A; 2J06 A; 3NPF A; 2SRC A; 2L0A A; 4DEX A; 4GBQ A; 1I0C A; 2RQV A; 1T3S A; 2GTJ A; 1PNJ A; 1B07 A; 4OMQ A; 2J6O A; 2YUP A; 1ABO A; 2GQI A; 1M3A A; 1BK2 A; 4F14 A; 2C0I A; 2BZY A; 4ZNX A; 1ARK A; 2L2P A; 4GLM A; 3EGU A; 3LH5 A; 2CSQ A; 1PRL C; 2J6K A; 2HBW A; 3VS6 A; 1ZBJ A; 2DF6 A; 1GFD A; 2RQW A; 4ORZ A; 5I11 A; 4F16 A; 1KSW A; 2ABL A; 1E6G A; 3NMZ C; 2DL7 A; 1NM7 A; 2DYB A; 2KNB B; 1B3Q A; 4IIO A; 2XMF A; 2HCK A; 4JZ4 A; 4J9H A; 1KJW A; 2KRN A; 2EYW A; 3PE0 A; 2LP5 A; 1RUW A; 1Y0M A; 5GJV B; 1X27 A; 2ECZ A; 3NGP A; 4K11 A; 3H0F A; 2LNH B; 3TVT A; 4AFU C; 1WXB A; 1AOJ A; 1UUE A; 1TUC A; 2L3Q A; 4J9G A; 1AWO A; 2A28 A; 2KEA A; 3I9Q A; 1PHT A; 3VS0 A; 1ABQ A; 1AZE A; ...
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Sperm-associated antigen 8 is a protein that in humans is encoded by the SPAG8 gene. The correlation of anti-sperm antibodies with cases of unexplained infertility implicates a role for these antibodies in blocking fertilization. Improved diagnosis and treatment of immunologic infertility, as well as identification of proteins for targeted contraception, are dependent on the identification and characterization of relevant sperm antigens. The protein encoded by this gene is recognized by sperm agglutinating antibodies from an infertile woman. This protein is localized in germ cells of the testis at all stages of spermatogenesis and is localized to the acrosomal region of mature spermatozoa. Alternatively spliced variants that encode different protein isoforms have been described but the full-length sequences of only two have been determined. GRCh38: Ensembl release 89: ENSG00000137098 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000066196 - Ensembl, May 2017 "Human PubMed Reference:". ...
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Plasminogen, the proenzyme of the fibrinolytically active enzyme plasmin, is a single chain glycoprotein with a molecular weight of about 90,000-94,000 Da (2). Various isoelectric forms exist and can be separated by means of isoelectric focusing (IEF).
According to the medical personnel of the AFU units (Ukrainian troops) there were recorded mass diseases among the Ukrainian military personnel in the field. Physicians recorded the unknown virus as a result of which the infected get the high fever which cannot be subdues by any medicines, and in two days there comes the fatal outcome. Thus far from the virus there have died more than twenty servicemen, what is carefully shielded by the commandment of the AFU from the publicity", said Basurin in daily MoD situation report ...
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Toshiba has begun shipping a 14TB helium-filled hard drive to clients, its largest capacity to date and the company's first foray into helium territory. Of course, helium-filled HDDs are not new, and WD already released a 14TB HDD a couple of months ago. However, Toshiba's is the industry's first HDD to pack nine disks inside, and the only 14TB drive to use conventional magnetic recording (CMR) technology.The new drive is part of Toshiba's MG07ACA series. It is available in both 12TB and 14TB capacities, both of which are CMR drives.We have raised the bar with the new MG07ACA Series 9-disk helium-sealed design, said Akitoshi Iwata, Vice President of Storage Products Division, Toshiba Electronic Devices and Storage Corporation. By utilizing an innovative design, we continue to improve the benefits that high-capacity disk storage can deliver to our broad global customer base.There are a couple of things to note about the 14TB model that make it sta
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A software developer now living in Copenhagen with interest in Biology, Bioinformatics, Computational Biology. rokhline/yahoo/com/au ...
TY - JOUR. T1 - Lysosomal dysfunction causes neurodegeneration in mucolipidosis II knock-in mice. AU - Kollmann, K.. AU - Damme, M.. AU - Markmann, S.. AU - Morelle, W.. AU - Schweizer, M.. AU - Hermans-Borgmeyer, I.. AU - Röchert, A. K.. AU - Pohl, S.. AU - Lübke, T.. AU - Michalski, J. C.. AU - Käkelä, R.. AU - Walkley, S. U.. AU - Braulke, T.. PY - 2012/9. Y1 - 2012/9. N2 - Mucolipidosis II is a neurometabolic lysosomal trafficking disorder of infancy caused by loss of mannose 6-phosphate targeting signals on lysosomal proteins, leading to lysosomal dysfunction and accumulation of non-degraded material. However, the identity of storage material and mechanisms of neurodegeneration in mucolipidosis II are unknown. We have generated knock-in mice with a common mucolipidosis II patient mutation that show growth retardation, progressive brain atrophy, skeletal abnormalities, elevated lysosomal enzyme activities in serum, lysosomal storage in fibroblasts and brain and premature death, ...
The coarse facial features have been described as "Hurler-like". Two major types have been described: type 1 with onset in the first 6 months of life and rapid psychomotor and general neurologic deterioration, and the later onset, less severe type 2 in which angiokeratomas resembling Fabry disease occur. Infants with type 1 may not survive beyond one year of age. The Hurler-like face is less pronounced and the neurologic deterioration is less rapid in type 2 with survival often into the third decade or later. The intracellular accumulation of glycolipids and glycoproteins leads to cell death accounting for the progression of CNS disease. Abnormal bone growth (dysostosis multiplex) can lead to short stature. Elevated sweat NaCl, hypohidrosis, and poor temperature control can be a feature of both types but this is more pronounced in type 1. The DNA mutation is the same in both types and there may be overlap in some of the clinical features. Furthermore, both types have been reported in the same ...
Mucopolysaccharidosis like inherited storage disorders. Four have been identified so far: muramidase deficiency (ML I), I cell disease (ML II), pseudo Hurler polydystrophy (ML III), and sialicosis (ML IV, also called fucosidosis). Abbreviated ML
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Calcium ions play a primary role in the regulation of sperm motility. This gene belongs to a family of putative cation channels that are specific to spermatozoa and localize to the flagellum. The protein family features a single repeat with six membrane-spanning segments and a predicted calcium-selective pore region. This gene is part of a tandem repeat on chromosome 15q15; the second copy of this gene is thought to be a pseudogene. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jan 2014 ...
Mucolipidosis II (I-cell disease) and mucolipidosis IIIA (classical pseudo-hurler polydystrophy) are caused by mutations in the GlcNAc-phosphotransferase alpha / beta -subunits precursor gene. Kudo M, Brem MS, Canfield WM Am J Hum Genet. 2006 Mar;78(3):451-63. For more information on Mucolipidosis II and mucolipidosis IIIA, please visit OMMBID Chapter 138. Thank you very much in advance […]. ...
Alpha-L-fucosidase is responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of ... Glycoside hydrolase family 29 includes alpha-L-fucosidases, They are lysosomal enzymes responsible for hydrolyzing the alpha-1, ... making alpha-l-fucosidases, the enzymes responsible for their processing, critically important. Deficiency in alpha-l- ... In human sperm, membrane-associated alpha-l-fucosidase is stable for extended periods of time, which is made possible by ...
Plasma alpha-L-fucosidase (see alpha-L-fucosidase) is an enzyme that in humans is encoded by the FUCA2 gene. GRCh38: Ensembl ... "Entrez Gene: FUCA2 fucosidase, alpha-L- 2, plasma". Narahara K, Tsuji K, Yokoyama Y, et al. (1991). "Specification of small ... 2001). "Cell surface human alpha-L-fucosidase". Eur. J. Biochem. 268 (11): 3321-31. doi:10.1046/j.1432-1327.2001.02237.x. PMID ... 1988). "Molecular biology of the alpha-L-fucosidase gene and fucosidosis". Enzyme. 38 (1-4): 45-53. PMID 2894306. Cordero OJ, ...
The gene encoding the alpha-fucosidase, FUCA 1, was found to be located to the short arm of chromosome 1p36 - p34, by Carrit ... If they are present, a skin or blood sample will be taken to test for below-normal amounts of alpha-fucosidase. - Fucosidosis ... The FUCA1 gene provides instructions for making an enzyme called alpha-L-fucosidase. The enzyme plays a role in the breakdown ... The deficiency of the enzyme alpha-L-fucosidase, which is used to metabolize complex compounds in the body (fucose-containing ...
Zhang SY, Lin BD, Li BR (2015). "Evaluation of the diagnostic value of alpha-l-fucosidase, alpha-fetoprotein and thymidine ...
"An alpha-L-fucosidase from Penicillium multicolor as a candidate enzyme for the synthesis of alpha (1-->3)-linked fucosyl ... Penicillium multicolor is an anamorph species of the genus of Penicillium which produces alpha-L-fucosidase, tilactase, ... Ajisaka, K.; Fujimoto, H.; Miyasato, M. (1998). "An α-l-fucosidase from Penicillium multicolor as a candidate enzyme for the ...
... alpha-galactosidase, N-acetyl-beta-glucosaminidase, alpha-mannosidase, alpha-fucosidase and esterase-lipase (C8) are negative. ... Acid is not produced from arabinose, N-acetylglucosamine, D-cellobiose, D-galactose, or methyl alpha-D-glucoside, lactose, D- ...
... alpha-L-fucosidase, poly(1,2-alpha-L-fucoside-4-sulfate) glycanohydrolase) is an enzyme with systematic name poly((1->2)-alpha- ... This enzyme catalyses the following chemical reaction Endohydrolysis of (1->2)-alpha-L-fucoside linkages in fucoidan without ...
2-alpha-L-fucosidase EC 3.2.1.64: 2,6-b-fructan 6-levanbiohydrolase EC 3.2.1.65: levanase EC 3.2.1.66: quercitrinase EC 3.2. ... 3-alpha-L-fucosidase EC 3.2.1.112: 2-deoxyglucosidase EC 3.2.1.113: mannosyl-oligosaccharide 1,2-a-mannosidase EC 3.2.1.114: ... 6-alpha-L-fucosidase EC 3.2.1.128: glycyrrhizinate beta-glucuronidase EC 3.2.1.129: endo-a-sialidase EC 3.2.1.130: glycoprotein ... alpha-agarase EC 3.2.1.159: alpha-neoagaro-oligosaccharide hydrolase EC 3.2.1.160: now EC 3.2.1.155 EC 3.2.1.161: beta-apiosyl- ...
Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks ... "Entrez Gene: FUCA1 fucosidase, alpha-L- 1, tissue". HPRD entry [1] Willems PJ, Gatti R, Darby JK, et al. (1991). "Fucosidosis ... Fukushima H, de Wet JR, O'Brien JS (1985). "Molecular cloning of a cDNA for human alpha-L-fucosidase". Proc. Natl. Acad. Sci. U ... Yang M, Allen H, DiCioccio RA (1993). "A mutation generating a stop codon in the alpha-L-fucosidase gene of a fucosidosis ...
... alpha-L-fucosidase MeSH D08.811.277.450.410 --- galactosidases MeSH D08.811.277.450.410.050 --- alpha-galactosidase MeSH ... gtp-binding protein alpha subunit, gi2 MeSH D08.811.277.040.330.300.200.100.300 --- gtp-binding protein alpha subunits, gq-g11 ... gtp-binding protein alpha subunits, g12-g13 MeSH D08.811.277.040.330.300.200.100.200 --- gtp-binding protein alpha subunits, gi ... steroid 12-alpha-hydroxylase MeSH D08.244.453.915.737 --- steroid 16-alpha-hydroxylase MeSH D08.244.453.915.748 --- steroid 17- ...
1,2-alpha-L-fucosidase 1,3-alpha-L-fucosidase 1,6-alpha-L-fucosidase FUCA2 Endreffy I, Bjørklund G, Szerafin L, Urbina MA, ... In enzymology, an alpha-L-fucosidase (EC 3.2.1.51) is an enzyme that catalyzes the chemical reaction an alpha-L-fucoside + H2O ... The systematic name of this enzyme class is alpha-L-fucoside fucohydrolase. This enzyme is also called alpha-fucosidase. This ... doi: 10.1007/s12026-017-8943-x. Levvy GA, Mcallan A (August 1961). "Mammalian fucosidases. 2. alpha-L-Fucosidase". The ...
... alpha/beta-galactosidase, β-glucuronidase, α-fucosidase, α-mannosidase, and trypsin. Important dual virulence factors found in ...
In enzymology, a 1,2-alpha-L-fucosidase (EC 3.2.1.63) is an enzyme that catalyzes the chemical reaction methyl-2-alpha-L- ... Other names in common use include almond emulsin fucosidase, and alpha-(1->2)-L-fucosidase. As of late 2007, 4 structures have ... 2-alpha-L-fucosidase". J. Biol. Chem. 245 (2): 299-304. PMID 5460888. Ogata-Arakawa M, Muramatsu T, Kobata A (1977). "alpha-L- ... Purification and properties of alpha-L-fucosidase from Chamelea gallina L". Eur. J. Biochem. 66 (2): 379-87. doi:10.1111/j.1432 ...
In enzymology, a 1,3-alpha-L-fucosidase (EC 3.2.1.111) is an enzyme that catalyzes the chemical reaction of cleaving the 1,3- ... Yoshima H, Takasaki S, Ito-Mega S, Kobata A (1979). "Purification of almond emulsin alpha-L-fucosidase I by affinity ... Ogata-Arakawa M, Muramatsu T, Kobata A (1977). "alpha-L-fucosidases from almond emulsin: characterization of the two enzymes ... The systematic name of this enzyme class is 3-alpha-L-fucosyl-N-acetylglucosaminyl-glycoprotein fucohydrolase. This enzyme is ...
This enzyme is also called alpha-L-fucosidase. Yazawa S, Madiyalakan R, Chawda RP, Matta KL (1986). "alpha-L-fucosidase from ... 6-alpha-L-fucosidase (EC 3.2.1.127) is an enzyme that catalyzes the chemical reaction Hydrolysis of 1,6-linkages between alpha- ... aspergillus niger: demonstration of a novel alpha-L-(1----6)-fucosidase acting on glycopeptides". Biochem. Biophys. Res. Commun ...
... beta-D-glucosides and alpha-L-arabinosides. Chinchetru, M.A.; Cabezas, J.A.; Calvo, P. (1983). "Characterization and kinetics ... Beta-D-fucosidase (EC 3.2.1.38, beta-fucosidase) is an enzyme with systematic name beta-D-fucoside fucohydrolase. This enzyme ... Beta-D-fucosidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ... Rodriguez, J.A.; Cabezas, J.A.; Calvo, P. (1982). "β-Fucosidase, β-glucosidase and β-galactosidase activities associated in ...
alpha-1,4-glucosidase activity. • alpha-glucosidase activity. Cellular component. • membrane. • lysosomal membrane. • lysosomal ... Acid alpha-glucosidase, also called α-1,4-glucosidase[5] and acid maltase,[6] is an enzyme (EC 3.2.1.20) that helps to break ... maltose alpha-glucosidase activity. • catalytic activity. • hydrolase activity. • carbohydrate binding. • isomaltase. • ... This gene encodes lysosomal alpha-glucosidase, which is essential for the degradation of glycogen to glucose in lysosomes. ...
... (EC 3.2.1.101, exo-1,6-beta-mannanase, endo-alpha-1-,6-D-mannanase, endo-1,6-beta-mannanase, ... mannan endo-1,6-beta-mannosidase, 1,6-alpha-D-mannan mannanohydrolase) is an enzyme with systematic name 6-alpha-D-mannan ... Random hydrolysis of (1-,6)-alpha-D-mannosidic linkages in unbranched (1-,6)-mannans. References[edit]. *^ Nakajima, T.; Maitra ... Mannan endo-1,6-alpha-mannosidase at the US National Library of Medicine Medical Subject Headings (MeSH) ...
Alpha-N-acetylgalactosaminidase *NAGA. *Alpha-N-acetylglucosaminidase. *Fucosidase. *Hexosaminidase *HEXA. *HEXB. *Iduronidase ...
EC 3.2.1.48 is sucrose alpha-glucosidase. Physiology[edit]. Sucrose intolerance (also known as congenital sucrase-isomaltase ...
Alpha-N-acetylgalactosaminidase *NAGA. *Alpha-N-acetylglucosaminidase. *Fucosidase. *Hexosaminidase *HEXA. *HEXB. *Iduronidase ...
OST is a component of the translocon in the endoplasmic reticulum (ER) membrane. A lipid-linked core-oligosaccharide is assembled at the membrane of the endoplasmic reticulum and transferred to selected asparagine residues of nascent polypeptide chains by the oligosaccharyl transferase complex.[3] The active site of OST is located about 4 nm from the lumenal face of the ER membrane.[4] It usually acts during translation as the nascent protein is entering the ER, but this cotranslational glycosylation is nevertheless called a posttranslational modification. A few examples have been found of OST activity after translation is complete.[5][6] Current opinion is that post-translational activity may occur if the protein is poorly folded or folds slowly.[6] ...
Alpha-fetoprotein. *Erythropoietin (EPO). Functions[edit]. Some functions served by glycoproteins[4]:524 Function Glycoproteins ...
1,2-alpha-L-fucosidase 1,3-alpha-L-fucosidase 1,6-alpha-L-fucosidase FUCA2 Endreffy I, Bjørklund G, Szerafin L, Urbina MA, ... In enzymology, an alpha-L-fucosidase (EC 3.2.1.51) is an enzyme that catalyzes the chemical reaction an alpha-L-fucoside + H2O ... The systematic name of this enzyme class is alpha-L-fucoside fucohydrolase. This enzyme is also called alpha-fucosidase. This ... doi: 10.1007/s12026-017-8943-x. Levvy GA, Mcallan A (August 1961). "Mammalian fucosidases. 2. alpha-L-Fucosidase". The ...
In enzymology, a 1,2-alpha-L-fucosidase (EC 3.2.1.63) is an enzyme that catalyzes the chemical reaction methyl-2-alpha-L- ... Other names in common use include almond emulsin fucosidase, and alpha-(1->2)-L-fucosidase. As of late 2007, 4 structures have ... 2-alpha-L-fucosidase". J. Biol. Chem. 245 (2): 299-304. PMID 5460888. Ogata-Arakawa M, Muramatsu T, Kobata A (1977). "alpha-L- ... Purification and properties of alpha-L-fucosidase from Chamelea gallina L". Eur. J. Biochem. 66 (2): 379-87. doi:10.1111/j.1432 ...
... alpha-fucosidase explanation free. What is alpha-fucosidase? Meaning of alpha-fucosidase medical term. What does alpha- ... Looking for online definition of alpha-fucosidase in the Medical Dictionary? ... Alpha-fucosidase , definition of alpha-fucosidase by Medical dictionary https://medical-dictionary.thefreedictionary.com/alpha- ... medical-dictionary.thefreedictionary.com/alpha-fucosidase,alpha-fucosidase,/a,. *Facebook ...
Crystal Structure of Thermotoga Maritima Alpha-L-Fucosidase. Insights Into the Catalytic Mechanism and the Molecular Basis for ... Alpha-L-fucosidase, putative 2336 3.2.1.51 , Details 4 1HL9 1 A, B PUTATIVE ALPHA-L-FUCOSIDASE ORF TM0306 2336 3.2.1.51 , ... Alpha-L-fucosidase, putative 2336 3.2.1.51 , Details 7 1HL8 1 A, B PUTATIVE ALPHA-L-FUCOSIDASE ORF TM0306 2336 3.2.1.51 , ... ALPHA-L-FUCOSIDASE, PUTATIVE 2336 3.2.1.51 , Details 14 1ODU 1 A, B PUTATIVE ALPHA-L-FUCOSIDASE ORF TM0306 2336 3.2.1.51 , ...
Inhibition of bovine kidney alpha-L-fucosidase by para-nitrophenolate release assay. ...
Involved in alpha-L-fucosidase activity. Specific Function. Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6- ... Showing Protein Plasma alpha-L-fucosidase (HMDBP00876). IdentificationBiological propertiesGene propertiesProtein properties ...
L-Fucosidase: Insights Into the Catalytic Mechanism and the Molecular Basis for Fucosidosis ... PUTATIVE ALPHA-L-FUCOSIDASE protein, length: 449 (BLAST) Sequence Similarity Cutoff. Rank. Chains in Cluster. Cluster ID / Name ... CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE IN COMPLEX WITH A MECHANISM BASED INHIBITOR. ...
Herein, a ratiometric fluorescent probe for the alpha-l-fucosidase (AFU) assay based on a single fluorophore has been developed ... Alpha-l-fucosidase (AFU) plays vital roles in some physiological processes that closely relate to several diseases. ... Alpha-L-fucosidase (AFU) plays vital roles in some physiological processes that closely relate to several diseases. Herein, a ... An anthracenecarboximide fluorescent probe for in vitro and in vivo ratiometric imaging of endogenous alpha-L-fucosidase for ...
Recombinant Protein and Alpha-fucosidase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are ... Alpha-fucosidase A. Alpha-fucosidase A ELISA Kit. Alpha-fucosidase A Recombinant. Alpha-fucosidase A Antibody. Also known as ... Alpha-fucosidase A (Alpha-L-fucoside fucohydrolase A).. Alpha-fucosidase involved in degradation of fucosylated xyloglucans. ... Alpha-fucosidase involved in degradation of fucosylated xyloglucans. Hydrolyzes alpha-1,2-linked fucose. Active on cotton ...
While the catalytic nucleophile in the configuration-retaining alpha-L-fucosidases from family GH29 is fully conserved with ... we largely confirm the acid/base residue predictions for the GH29 fucosidases from the two subfamilies. ...
Inhibition of bovine epididymis alpha-L-fucosidase assessed as p-nitrophenol release at 1000 uM at pH 5.5 by spectrometric ...
Recombinant Protein and Probable alpha-fucosidase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody ... Probable alpha-fucosidase A. Probable alpha-fucosidase A ELISA Kit. Probable alpha-fucosidase A Recombinant. Probable alpha- ... fucosidase A Antibody. Also known as Probable alpha-fucosidase A (Alpha-L-fucoside fucohydrolase A).. Alpha-fucosidase involved ... Hydrolyzes alpha-1,2-linked fucose (By similarity).. Below are the list of possible Probable alpha-fucosidase products. If you ...
Rat monoclonal Antibody to alpha-L-Fucosidase. Clone. ALF89. Immunogen. Alpha-L-Fucosidase from human liver (51 kDa & 56 kDa ...
... rat sperm alpha-L-fucosidase was characterized during epididymal maturation. The pH 7 activity optimum of alpha-L-fucosidase ... alpha-L-Fucosidase from sperm from the distal half of the cauda, which contained a significant enrichment of sperm and alpha-L- ... Isoelectric focusing of alpha-L-fucosidase indicated the presence of a major isoform (B) with a pI near 7 in sperm from testis ... Neuraminidase treatment of sperm alpha-L-fucosidase from distal cauda (when compared with the appropriate heat-treated control ...
2-alpha-l-fucosidase (AfcA) was isolated. The afcA gene was found to comprise 1,959 amino acid residues with a predicted ... A domain responsible for fucosidase activity (the Fuc domain; amino acid residues 577 to 1474) was localized by deletion ... The recombinant Fuc domain specifically hydrolyzed the terminal alpha-(1--,2)-fucosidic linkages of various oligosaccharides ... genomic library of Bifidobacterium bifidum constructed in Escherichia coli was screened for the ability to hydrolyze the alpha ...
2-L Fucosidase specifically cleaves the alpha 1,2 fucoside bond, liberating L-fucose from 22-alpha-L-fucosyl lactose (Fuc ... N-glycan degradation: Alpha 1,2-L Fucosidase Alpha 1,2-L Fucosidase specifically cleaves the alpha 1,2 fucoside bond, ... Substrate specificity of alpha 1,2-L-fucosidase (Cat.# 4451). Substrate specificity of alpha 1,2-L-fucosidase (Cat.# 4451). ... Alpha 1,2-L-Fucosidase. 2 Units. USD $402.00 Intended usage: Specific cleavage of α1,2-L-fucoside bonds. This enzyme releases L ...
Fucosidosis is an autosomal recessive lysosomal storage disorder caused by reduced or absent alpha-L-fucosidase enzyme activity ... enzyme analysis of alpha-L-fucosidase can confirm the diagnosis. ... Alpha-Fucosidase, Leukocytes Reporting Name. Alpha-Fucosidase, ... 3. Thomas GH: Disorders of Glycoprotein Degradation: alpha-Mannosidosis, beta-Mannosidosis, Fucosidosis, and Sialidosis. In The ...
OMIM: FUCOSIDASE, ALPHA-L, 1. *. Willems PJ, Gatti R, Darby JK, Romeo G, Durand P, Dumon JE, OBrien JS. Fucosidosis revisited ... alpha-L-fucosidase 1. Enable Javascript to view the expand/collapse boxes.. Printable PDF Open All Close All ... The FUCA1 gene provides instructions for making an enzyme called alpha-L-fucosidase. This enzyme is found in lysosomes, which ... Most of these mutations result in an abnormally short, nonfunctional alpha-L-fucosidase enzyme. Without this enzyme, ...
Activity-based screening of a genomic library was used to isolate the gene encoding a novel α-L-fucosidase. The enzyme was ... As a very low amino acid sequence similarity with known α-l-fucosidases was found, following study could be important for ... In this study, new enzyme α-l-fucosidase iso2 originating from Paenibacillus thiaminolyticus was described and prepared in ... Hydrolytic and transglycosylation abilities of α-l-fucosidase iso2 were tested using different acceptor molecules. ...
Alpha-L-Fucosidase 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene ... Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of ... Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of ... This gene encodes a plasma alpha-L-fucosidase, which represents 10-20% of the total cellular fucosidase activity. The protein ...
Alpha-L- 1, Tissue, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene ... R&D Systems Antibodies for FUCA1 (Tissue alpha-L-Fucosidase/FUCA1). *R&D Systems Proteins and Enzymes for FUCA1 (Tissue alpha-L ... Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of ... Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of ...
The FUCA1 gene provides instructions for making an enzyme called alpha-L-fucosidase. Learn about this gene and related health ... The FUCA1 gene provides instructions for making an enzyme called alpha-L-fucosidase. This enzyme is found in lysosomes, which ... Most of these mutations result in an abnormally short, nonfunctional alpha-L-fucosidase enzyme. Without this enzyme, ... Alpha-L-fucosidase is responsible for cutting (cleaving) off a sugar molecule called fucose toward the end of the breakdown ...
FUCA1: alpha-L-fucosidase 1. *FUS: FUS RNA binding protein. *FXN: frataxin ...
Alpha-L-rhamnosidase (IPR016007). *Alpha-L-fucosidase (IPR016518). *Maltose phosphorylase/glycosyl hydrolase/vacuolar acid ... The six-hairpin glycoside transferase domain, with an alpha/alpha toroid fold, contains six alpha-hairpins arranged in closed ...
Tissue alpha-L-fucosidase (IPR028755). *Exo-beta-D-glucosaminidase (IPR028829). *Chitinase insertion domain superfamily ( ... This entry represents the catalytic TIM beta/alpha barrel common to many different families of glycosyl hydrolases found in all ... Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of ... such as alpha-amylase) [PMID: 11914097], beta-glycanases [PMID: 14668328], family 1 glycosyl hydrolases (such as beta- ...
  • Stabilization of membrane-associated alpha-L-fucosidase by the human sperm equatorial segment. (semanticscholar.org)
  • In human sperm, membrane-associated alpha-l-fucosidase is stable for extended periods of time, which is made possible by membrane domains and compartmentalisation. (embl.de)
  • While the catalytic nucleophile in the configuration-retaining alpha-L-fucosidases from family GH29 is fully conserved with respect to sequence, there is no fully sequence-conserved acid/base residue candidate across the family. (ubc.ca)
  • Through comparison of kinetic parameters obtained for the hydrolysis of fucosyl substrates with activated leaving groups by these mutants with those of the corresponding wild-type enzymes, in conjunction with the demonstration of azide rescue, we largely confirm the acid/base residue predictions for the GH29 fucosidases from the two subfamilies. (ubc.ca)
  • In order to utilize fucosylated oligosaccharides, ATCC 15697 possesses several fucosidases, implicating GH29 and GH95 α- l -fucosidases in a gene cluster dedicated to HMO metabolism. (asm.org)
  • Finally, the HMO cluster GH29 α- l -fucosidase possesses a crystal structure that is similar to previously characterized fucosidases. (asm.org)
  • The afcB gene encodes a 1493-amino acid polypeptide containing an N-terminal signal sequence, a GH29 - l -fucosidase domain, a carbohydrate binding module (CBM) 32 domain, a found-in-various-architectures (FIVAR) domain and a C-terminal transmembrane region, in this order. (scialert.net)
  • AXY8 encodes an alpha-fucosidase, underscoring the importance of apoplastic metabolism on the fine structure of Arabidopsis cell wall polysaccharides. (mpg.de)
  • Using a new promoter analysis transformation vector for Dictyostelium discoideum (PAV-CAT), we have defined cis-acting elements in the promoter of the cyclic AMP-induced early-expressed gene A11H2, which encodes an alpha-fucosidase-related protein (A. Müller-Taubenberger, M. Westphal, A. Noegel, and G. Gerisch, FEBS Lett. (asm.org)
  • Sensitive carbohydrate chemistry techniques require specific enzymes such as fucosidase, sialidase, biosidase, and other hydrolytic enzymes with activities specific for certain linkages. (cellartis.com)
  • Precise, pure enzymes from Takara Bio for carbohydrate chemistry analyses include alpha-1,2 fucosidase, alpha-1,3/1,4 fucosidase, alpha 2,3-sialidase, Lacto-N-biosidase, and glycan hydrolases useful for sphingolipid analysis such as recombinant endoglycoceramidase II. (cellartis.com)
  • α- l -Fucosidases are enzymes involved in metabolism of α- l -fucosylated molecules, compounds with a fundamental role in different life essential processes including immune response, fertilization and development, but also in some serious pathological events. (biomedcentral.com)
  • Fucosylated glycoconjugates are involved in numerous biological events, making alpha-l-fucosidases, the enzymes responsible for their processing, critically important. (embl.de)
  • Despite this, few studies have focussed on xyloglucan saccharification, which requires a consortium of enzymes including endo-xyloglucanases, alpha-xylosidases, betagalactosidases and alpha-l-fucosidases, among others. (proteopedia.org)
  • Using a genomic library of Paenibacillus thiaminolyticus , constructed in E.coli DH5α cells, nucleotide sequence of a new α- l -fucosidase isoenzyme was determined and submitted to the EMBL database (HE654122). (biomedcentral.com)
  • Differences in the isoenzyme pattern of alpha-L-fucosidase were found in chorionic villi and maternal decidua. (ac.ke)
  • Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Thermotoga maritima through trapping of a covalent glycosyl-enzyme intermediate and mutagenesis. (semanticscholar.org)