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At least 19 recordsLinked to original sources
PubMed1976

Physico-chemical and immunological properties of acid alpha-glucosidase from various human tissues in relation to glycogenosis type II (Pompe's disease).

The physico-chemical and immunological properties of acid alpha-glucosidase from various human tissues have been studied. Heat stability of acid alpha-glucosidase from heart, liver and skeletal muscle is identical, but for kidney some different results are obtained. Identical isoelectrofocussing patterns are found for heart, liver and skeletal muscle. Furthermore, the effect of antiserum against human liver acid alpha-glucosidase on the activity of acid alpha-glucosidase from various tissues is studied. The results are discussed in relation to glycogenosis type II (Pompe's disease).

Antigen-Antibody Reactions↗
PubMed1976

Two alpha-glucosidases in cultured amniotic fluid cells and their differentiation in the prenatal diagnosis of Pompe's disease.

A sensitive fluorometric assay utilizing 4-methylumbelliferyl-alpha-D-glucopyranoside has been developed for the determination of alpha-glucosidase. The enhanced sensitivity was achieved by increasing the solubility of the substrate with a water miscible organic solvent. With this system, cultured amniotic fluid cells were found to have two major forms of alpha-glucosidase with somewhat overlapping acidic pH optima; one with pH optimum at 4.5 is deficient in Pompe's disease (type II glycogenosis), while one with pH optimum at 6.0 is not affected in this disease. Specificity for the pH 4 form of alpha-glucosidase was achieved by exploiting the greater thermal lability of the pH 6 enzyme. The pH 6 form of the enzyme was also detectable in freshly prepared extracts of cultured fibroblasts. The procedure is direct and simple and has been applied to the prenatal diagnosis in two pregnancies at risk for Pompe's disease.

Amniotic Fluid↗
PubMed1976

Production of extracellular alpha-glucosidase by a thermophilic Bacillus species.

Production of extracellular alpha-glucosidase was studied with strain KP 1006 of a new species of thermophilic Bacillus, which was isolated from soil samples by enrichment at 65 C. alpha-Glucosidase production was maximum at 60 C and at an initial pH of 6.5. The final enzyme yield was increased by starch, maltose, glycerol, peptone, and yeast extract but reduced by acetate and gluconate, alpha-Glucosidase was formed in the cytoplasm and accumulated as a large pool during the logarithmic growth phase. At a midpoint of this period, the enzyme appeared in the culture broth, and its level increased until the end of the stationary phase.

Bacillus↗
PubMed1976

[Alpha-glucosidase from human kidneys].

The data obtained show that most part of the activity of neutral alpha-glucosidases from human kidney is observed in the particle fraction, and only approximately 15%--in supernatant. Soluble neutral alpha-glucosidases have at least 4 different forms, as it is shown by means of their fractionation on Sephadex G-150, Bio-Gel P-200 and by polyacrylamide gel electrophoresis. Four forms are different in their molecular weight, electrophoretic mobility and substrate specificity. Two of the forms have molecular weight of 310000 and 110000. All the neutral alpha-glucosidases except high molecular weight form (greater than 400000) were retarded on column of Sephadex G-150.

Catalysis↗
PubMed1976

Purification and properties of extracellular alpha-glucosidase of a thermophile, Bacillus thermoglucosidus KP 1006.

An extracecular alpha-glucosidase (alpha-D-glucoside glycohydrolase, EC 3.2.1.20) of a thermophile, Bacillus thermoglucosidius KP 1006, was purified about 350-fold. The purified enzyme had a specific activity of 164 mumol of p-nitrophenyl-alpha-D-glucopyranoside hydrolyzed per min at 60 degrees C and pH 6.8 per mg of protein. The molecular weight was estimated at 55 000. The pH and temperature optima for activity were 5.0--6.0 and 75 degrees C, respectively. Below 40 degrees C, the activity was less than 4.5% of the optimym. The enzyme showed a high specificity for alpha-D-glucopyranoside. The maximal hydrolyzing velocity per substrate diminished in the order: phenyl-alpha-D-glucopyranoside, p-nitrophenyl-alpha-D-glucopyranoside, isomaltose, methyl-alpha-glycopyranoside. The respective Km values were 3.0, 0.23, 3.2 and 27 mM. The activity was trace for turanose, and not detectable for sucrose, trehalose, raffinose, melezitose, maltose, maltotriose, phenyl-alpha-D-maltoside, dextran, dextrin and starch. Tris, p-nitrophenyl-alpha-D-xylopyranoside, glucose and glucono-delta-lactone blocked competitively the enzyme with respect to p-nitrophenyl-alpha-D-glucopyranoside. The Ki values were 0.12, 0.14, 2.2 and 2.4 mM, respectively. The activity was affected by heavy metal ions, but insensitive to EDTA, p-chloromercuribenzoate and iodoacetate. The enzyme was stable up to 60 degrees C, and inactivated rapidly at temperatures beyond 72 degrees C. The pH range for stability was 4.0--11.0 at 31 degrees C, and 6.0--8.5 at 55.5 degrees C. At 25 degrees C, the enzyme failed to be inactivated in 45% ethanol, in 7.2 M urea, and in 0.06% sodium dodecyl sulfate, but the tolerance was extremely reduced at 60 degrees C.

Bacillus↗
PubMed1977

[Catalytic properties of a neutral alpha-glucosidase from human kidney].

The catalytic properties of a neutral alpha-glucosidase purified to homogeneity from human renal cortex are described. The pH optimum was 6 (maltose and starch). It has a broad range of substrate specificity, hydrolysing di- and oligosaccharides with alpha (1 leads to 2), alpha (1 leads to 3), alpha (1 leads to 4) and alpha (1 leads to 6) linkages. Glucosidase action on maltosaccharides was associated with pronounced substrate inhibition at concentrations exceeding 0,5 mM. It also hydrolyses polysaccharides as starch and glycogen. The Km and Vmax values for the various substrates were determined. The enzymes exhibited intrinsic transglucosylase activity. It catalysed glucosyl-transfer reaction from maltose to itself (disproportionation). Mixed substrate inhibition studies, inhibition studies and heat inactivation are interpreted in terms of the existence of at least two interacting sites on the enzyme.

Drug Stability↗
PubMed1976

Normal limits of urinary excretion of eleven enzymes.

Urinary excretion of lactate dehydrogenase, hydroxybutyrate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, arylsulphatase A, alpha-glucosidase, beta-galactosidase, trehalase, N-acetyl-beta-glucosaminidase, beta-glucuronidase, and leucinearylamidase was studies in a carefully selected group of 100 healthy subjects, 50 women and 50 men. Enzyme activities were assayed in 3-h morning samples after gel filtration of the urine. Activities were related to time volume, and to urinary creatinine concentration. Several transforming functions had to be applied to enzyme output data to obtain an approximation to gaussian frequency distribution. Men showed a significantly higher excretion of gamma-glutamyltransferase, alpha-glucosidase, trehalase, N-acetyl-beta-glucosaminidase,beta-glucuronidase, and leucine arylamidase activity than did women if enzyme activity was related to urinary time volume. Women excreted more lactate dehydrogenase, hydroxybutyrate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, alpha-glucosidase, trehalase, and N-acetyl-beta-glucosaminidase activity than did men, if urinary creatinine was used as the basis of reference. Reference intervals were calculated as 2.5 and 97.5 percentiles for both sexes.

Acetylglucosaminidase↗
PubMed1977

Enzyme activities in human liver biopsies: assay methods and activities of some lysosomal and membrane-bound enzymes in control tissue and serum.

1. Highly sensitive technique are described for the assay of plasma membrane (5'-nucleotidase, alkaline phosphatase), microsomal (neutral alpha-glucosidase, leucyl-2-naphthylamidase) and biliary canalicular (gamma-glutamyltransferase) enzymes and for nine acid hydrolases (acid phosphatase, phosphodiesterase, beta-glucosidase, alpha-glucosidase, alpha-galactosidase, beta-galactosidase, alpha-mannosidase, N-acetyl-beta-glucosaminidase, beta-glucuronidase) in human liver. 2. Optimum and specific assay systems have been developed which give linear kinetics for all enzymes. 3. The range of enzyme activities in samples of human liver, obtained by closed needle biopsy, and sera have been determined.

Alkaline Phosphatase↗
PubMed1976

Starch degradation by the mould Trichoderma viride. I. The mechanism of starch degradation.

The mechanism of starch degradation by the fungus Trichoderma viride was studied in strain CBS 354.44, which utilizes glucose, starch and dextrins but is unable to assimilate maltose. It was shown that the amylolytic enzyme system is completely extracellular, equally well induced by starch, amylose or amylopectin and that it consists mainly of enzymes of the glucoamylase type which yield glucose as the main product of starch hydrolysis. Small amounts of alpha-amylase are produced also. The enzymes produced in starch cultures degrade starch, amylose and amylopectin equally well. Enzyme synthesis in starch media takes place to a considerable extent after exhaustion of the carbon source when maximum growth has been attained. Low-molecular dextrins are degraded by extracellular enzymes of the glucoamylase type. These enzymes are produced in media containing starch or dextrins. Maltotriose is consumed for only one third leaving maltose in the culture filtrate. Maltose is hardly attacked and hardly induces any amylolytic enzyme activity. No stable alpha-glucosidase appears to be produced.

Amylases↗
PubMed1976

A microfluorometric assay of leukocyte alpha-1,4-glucosidase.

We describe an improved method for detecting deficiency of the acid hydrolase, alpha-1,4-glucosidase in leukocytes, the enzyme defect in glycogen storage disease Type II (Pompe disease). The procedure requires smaller volumes of blood and less time than previous methods. The assay involves the separation of leukocytes by Peter's method for beta-glucosidase and a modification of Salafsky and Nadler's fluorometric method for alpha-glucosidase.

Adult↗
PubMed2026

Genomic profiling of digestion related enzymes in Anopheles aquasalis a major coastal neotropical malaria vector.

Digestive genes are fundamental for the development and survival of mosquitoes and can serve as a target for the development of strategies for mosquito control or vector-borne disease prevention. Genes related to digestion were identified in the genome of the neotropical malaria vector Anopheles aquasalis by similarity. We used reciprocal BLAST with annotated digestion proteins for Anopheles gambiae. Orthology and evolutionary analyses were performed using MEGA with a bootstrapped phylogenetic tree constructed by the neighbor-joining method, and copy number variation was measured by the standard deviation of the average copy number in each gene family. We identified 241 genes related to digestion in An. aquasalis: 56 genes related to carbohydrate digestion, 51 genes for lipid digestion, and 134 genes for protein digestion. Phylogenetic relationships with other anophelines show that An. aquasalis genes are closely related to those of neotropical mosquitoes Anopheles darlingi and Anopheles albimanus. Orthologous gene clusters are conserved in important families of all four species. Some of these conserved genes are of interest for studies on controlling mosquito vectors, such as larvicidal toxin receptor genes, alpha-amylase, alpha-glucosidase, and maltase; important target genes for transmission-blocking vaccines, such as aminopeptidase N1 and carboxypeptidase B; and the major intestinal serine proteases, such as trypsins and chymotrypsins, which can positively or negatively affect Plasmodium development in the midgut. These data provide a better understanding of digestion-related genes in American anopheline mosquitoes and may support further fundamental and applied studies aimed at malaria control.

Animals↗
PubMed1976

Acid hydrolases in leukocytes and platelets of normal subjects and in patients with Gaucher's and Fabry's disease.

Lymphocytes, monocytes, neutrophilic granulocytes and platelets were each separated to greater than 95% purity from six normal subjects, three patients with Gaucher's disease, two heterozygotes for Gaucher's disease, and one patient with Fabry's disease. Activities of the following acid hydrolases were determined: "acid" (pH 4.0) beta-glucosidase, pH 5.0 beta-glucosidase, alpha-galactosidase, alpha-arabinosidase, alpha-mannosidase, alpha-glucosidase, beta-glucuronidase, beta-galactosidase, beta-hexosaminidase, and acid phosphatase. Enzymatic activity varied greatly with cell type and the enzyme being measured; the importance of assaying pure preparations especially for heterozygote detection is emphasized. Gaucher's disease patients' cells were found to be deficient in the pH 4.0 acid beta-glucosidase, variable in the pH 5.0 beta-glucosidase, and normal in all other acid hydrolases tested, including acid phosphatase, the activity of which is known to be elevated in plasma. Blood cells of a patient with Fabry's disease were deficient in alpha-galactosidase and normal in all other acid hydrolases tested.

Acid Phosphatase↗
PubMed1976

Rapid diagnosis of Enterobacteriaceae. I. Detection of bacterial glycosidases.

The paper describes a number of tests for the rapid detection of glycosidases including alpha-glucosidase, beta-glucosidase, beta-glucuronidase, beta-xylosidase and alpha-fucosidase. The methods use heavy suspensions of viable but non-multiplying bacteria in a buffered solution of a chromogenic substrate. The results of the tests are readable within 4 h. The application of these tests to a collection of 633 strains of Enterobacteriaceae and Vibrionaceae demonstrates that some of the tests may be valuable additions to the present tests available for the identification of bacteria belonging to these families. beta-glucuronidase activity was observed only in strains of the Escherichia-Shigella group. 97 per cent of the Escherichia strains possessed beta-glucuronidase activity. beta-xylosidase activity was almost completely restricted to strains of the Klebsiella-Enterobacter group in addition to Yersinia strains. None of the strains possessed alpha-fucosidase activity.

Bacteriological Techniques↗
PubMed1976

Physical, chemical, and enzymatic studies on the major sucrase of honey bees (Apis mellifera).

A sucrase from honey bees (Apis mellifera) which precipitates between ammonium sulfate saturations of 50 and 70% (5 mg protein per millilitre) and which makes up the major portion of the sucrases of honey bees was purified to homogeneity as shown by several criteria. A large part of the sucrase was found in the head while most of the rest was in the abdomen (a small amount was in the thorax). The enzyme precipitated between the same values of ammonium sulfate saturation as did the sucrase in honey and honey sucrase exhibited kinetics very similar to those of this enzyme. The enzyme was found to be a relatively nonspecific alpha-glucosidase and was shown to have transglucosidase activity. The production of glucose from sucrose was rectilinear when plotted by the Hofstee method at low substrate concentrations but decreased at high sucrose concentrations. The production of fructose was rectilinear throughout the concentration range used. The production of both glucose and rho-nitrophenol when rho nitrophenyl alpha-D-glucoside was the substrate was linear by the Hofstee plot. These effects were found to be due to transglucolysis and a mechanism of action is proposed. Amino acid and amino sugar analyses indicated that the sucrase was a glycoprotein. The molecular weight was found to be between 51000 and 82000 by three different methods and an so20.w value of 4.0 S was obtained. There was no evidence for subunit structure. Tests of the enzyme under various denaturation conditions did not reveal any unusual stabilities. The sucrase bound very tightly to a hydrophobic column. Iodoacetic acid decreased the activity of the sucrase but a large concentration was needed to bring about a 50% activity loss. Reducing agents caused some activity declines. Diethyl pyrocarbonate activated the enzyme.

Amino Acids↗
PubMed1977

The purification and characterization of rat liver lysosomal alpha-L-fucosidase.

The alpha-L-fucosidase from rat liver lysosomes was purified approximately 27,000-fold (from cytoplasmic extract) by a rapid procedure requiring only 7 h anf providing enzyme in a 20 per cent yield. The procedure is based upon affinity chromatography with agarose-epsilon-aminocaproyl-fucosamine. The isolated enzyme was found to be pure by a number of different analytical gel techniques and is essentially free of other lysosomal gylcosidases. The purified enzyme exhibits a positive periodic acid-Schiff stain, suggesting that it is a glycoprotein. The purified enzyme has a pH optimum of 5.7 to 5.9, a Vmax of 27 mumol/min/mg of protein, and a Km of 0.19 mM with p-nitrophenyl alpha-L-fucopyranoside as substrate. L-Fucose was the only possibly physiological effector of the enzyme which was identified; it exhibited a Ki of 1.6 mM, with p-nitrophenyl alpha-L-fucopyranoside as substrate. The enzyme has a subunit molecular weight of approximately 55,000 by Na dodecyl-SO4 electrophoresis in a variety of gel systems. The molecular weight of the native enzyme was indicated to be approximately 160,000 by sucrose density centrifugation, 300,000 by molecular sieve chromatography on Sephadex G-200, and 217,000 by sedimentation equilibrium centrifugation. The weight of evidence suggests that the enzyme is a tetramer. Incubation on the absence of sulfhydryl reagents under appropriate conditions generates a second alpha-L-fucosidase activity band on gels corresponding to a molecular weight of approximately 40,000 to 50,000. This result suggests that the subunit is relatively stable and may reassociate to form active enzyme. Alpha-L-Fucosidase requires a high concentration of protein and the presence of a sulfhydryl reagent for stabilization. It is rapidly inactivated by p-chloromercuriphenyl sulfonic acid, this inactivation being rapidly reversible by the addition of 10 mM 2-mercaptoethanol. The enzyme catalyzed the hydrolysis of 1 leads to 2, 1 leads to 3, and 1 leads to 4 fucosyl linkages and was found to be active on glycopeptides but not on native glycoproteins. The amino acid and carbohydrate composition of the enzyme was determined. The native enzyme contains the following sugars (residues per tetramer): fucose (3.5), mannose (32), galactose (8), glucose (9), glucosamine (32), and sialic acid (8). Rat liver lysosomal alpha-glucosidase, also produced in the rapid isolation procedure described herein, contained less than 0.1 residue of sialic acid per subunit.

Amino Acids↗
PubMed1975

[The effect of therapeutic gentamycin doses on the enzyme secretion in urine].

8 patients with chronic pyelonephritis were given gentamycin intramuscularly injected in individual dosage during 8-10 days. Here the behaviour of the excretion of protein, alanine aminopeptidase alkaline phosphatase, alpha-glucosidase, gamma-glutamyl transpeptidase and lysozyme with the urine was tested. With the exception of the lysozymuria, which increased only in patients with chronic renal insufficiency, regularly a hyperenzymuria developed. Most distinctly the excretion of the alanine aminopeptidase increased. After initial decrease the excretion of total protein transiently increased after completion of the gentamycin therapy. All the deviations were reversible. From the increased excretion of enzymes may not be concluded to a nephrotoxicity of gentamycin.

Alkaline Phosphatase↗
PubMed2026

Design, synthesis and biological evaluation of hydroxybenzothiazole-linked benzothiazole/benzoxazole conjugates as potent dual α-amylase and α-glucosidase inhibitors.

The current study focuses on the synthesis and evaluation of novel Hydroxybenzothiazole-Linked Benzothiazole/Benzoxazole Conjugates to target Diabetes Mellitus (DM) by inhibiting α-amylase and α-glucosidase. Spectroscopic methods, including 1H and 13C NMR spectroscopy, were employed to confirm the structures of newly synthesized conjugates. The findings of in-vitro analysis displayed that the synthesized derivatives inhibited α-amylase and α-glucosidase enzymes with IC50 values ranging from 3.65 ± 0.20 μM to 32.15 ± 3.20 μM on α-amylase and 5.92 ± 0.80 μM to 35.60 ± 3.40 μM on α-glucosidase, in contrast to the reference drug Acarbose (α-amylase IC50 = 8.25 ± 0.80 μM; α-glucosidase IC50 = 10.75 ± 1.10 μM). Among the series 9a-9f and 10a-10f, analogs 10 f, 10b, 9b, and 9e displayed superior anti-diabetic activity compared to the reference drug Acarbose. The inhibitory activity of these conjugates can be attributed to their favorable and stable interactions with critical amino acid residues of targeted enzymes, as revealed through molecular docking analysis. ADMET predictions and drug-likeness evaluations showed favorable pharmacokinetic features, while DFT investigations revealed electronic insights related to bioactivity. Experimental outcomes and in silico support display that these potent Hydroxybenzothiazole-Linked Benzothiazole/Benzoxazole Conjugates were comparable to an existing diabetic mellitus inhibitor while conserving an acceptable safety profile, specifying potential for further therapeutic development and optimization against diabetic Mellitus.

Benzothiazoles↗
PubMed2025

Reduction of false-positive results with biochemical second-tier testing for newborn screening of Pompe disease.

PURPOSE: To review the performance and outcomes of a second-tier newborn screening test for Pompe disease. METHODS: We followed our previously published screening approach that reduces false-positive results by incorporating creatine and creatinine levels and postanalytic tools in a second-tier test. RESULTS: We reviewed 1879 blood samples from neonates born in 11 states. Second-tier testing effectively reduced false-positive results, compared with first-tier enzyme testing alone. Only a small number of screen-positive cases (n = 7) were confirmed to have infantile-onset Pompe disease. No false-negative cases of infantile-onset Pompe disease were identified in this cohort, and 6 cases of possible late-onset Pompe disease were not detected with this approach. CONCLUSION: This tiered screening strategy discriminated well between true- and false-positive results and improved the positive predictive value. However, it did not reliably differentiate between infantile- and late-onset Pompe disease.

Humans↗