Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Optimal assay conditions are described for plasma alpha-galactosidase, beta-glactosidase, beta-glucuronidase, alpha-mannosidase, alpha-glucosidase, N-acetyl-beta-glucosaminidase, alpha-fucosidase, N-acetyl-alpha-glucosaminidase, acid phosphatase and arylsulphatase A. The levels of these activities in normal adults and children, and the stabilities of the activities on storage at -20 degrees C or 4 degrees C, are reported. The levels of these enzymic activities in plasma from patients with Fabry, Pompe, Sanfilippo A, Sanfilippo B, Tay Sachs and Hunter diseases, GM1-gangliosidosis and metachromatic leucodystrophy are described, and the possibility of using plasma hydrolase activities in the diagnosis of these conditions is discussed.
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PMID:Plasma acid hydrolases in normal adults and children, and in patients with some lysosomal storage diseases. 3 Dec 50

Saccharomyces carlsbergensis strain ATCC 9080 was grown on acid hydrolyzed brewery waste. The substrate contains 22 mg/ml of total carbohydrates of which approximately 60% represents reducing sugars such as maltose and glucose. Optimal conditions for substrate hydrolysis were 1.5% w/v sulfuric acid, 20 minutes and temperature of 110 degrees C. Maximum enzyme production was obtained in a medium containing 0.05% w/v yeast extract at 35 degrees C and at an initial pH of 6. Addition of nitrogen sources was unnecessary. Optimal conditions for alpha-glucosidase extraction from yeast included pH 7.5, 30 degrees C, and 10 minutes of sonication. Maximum hydrolysis of PNPG occurred at pH 7.5, temperature between 30 degrees C and 25 minutes of incubation. Michaelis-Menten constants and Vmax were 1 mM, 0.56 mol/min/mg of protein on P-nitrophenly-alpha-D-glucophyra-noside and 5 mV, 5 mol/min/mg of protein on maltose respectively.
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PMID:Production of intracellular alpha-glucosidase in brewery waste by Saccharomyces carlsbergenesis. 270 Jan 12

Most biological fluids contain both neutral and acid alpha-glucosidase. Optimal conditions were therefore developed for the selective determination of the activity of neutral and acid alpha-glucosidase, using 2-step, discontinuous assays. In the first step of the assay of neutral alpha-glucosidase, glucose was liberated from maltose (citrate-phosphate buffer, pH 6.8, 20 mmol/l maltose, 25 mmol/l turanose). Under these incubation conditions, turanose inhibited the residual activity of acid alpha-glucosidase almost completely without influencing the activity of neutral alpha-glucosidase. In the first step of the acid alpha-glucosidase assay, glucose was liberated from maltose (citrate-phosphate buffer, pH 3.8, 50 mmol/l maltose, 2 mol/l potassium chloride). Under these incubation conditions, potassium ions stimulate the activity of acid alpha-glucosidase and simultaneously inhibit almost completely the residual activity of neutral alpha-glucosidase. In the second step of the assay of neutral and acid alpha-glucosidase, the liberated glucose was measured by hexokinase/glucose-6-phosphate dehydrogenase. The effect of turanose and potassium ions on neutral and acid alpha-glucosidase from human urine was characterized.
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PMID:Selective determination of the activities of neutral and acid alpha-glucosidase using discontinuous assays. 635 65

Treatment of couple infertility due to male subfertility by means of intra-uterine insemination (IUI) gives better results, in terms of per cycle and total cumulative pregnancy rate, if sperm preparation is performed using a discontinuous Percoll gradient than if centrifugation-resuspension is used. Also, the minimal semen requirements for successful IUI are lower with the former technique. Optimal epididymal function, with total alpha-glucosidase activity in seminal plasma > 83 IU/mL or Schorr stain result > 60%, is associated with a high probability of success of IUI [odds ratio (OR) = 11.1 and 9.4 respectively; p < 0.01]. If semen contains > 2.3 million white blood cells per mL or more than 13 million spermatozoa/mL with grade a motility the success rate is decreased (OR = 0.25 and 0.30 respectively; p < 0.05 and p < 0.01). It is concluded that IUI is a highly successful treatment in specific cases of male subfertility, provided that the correct technique of sperm preparation is used.
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PMID:Statement on intra-uterine insemination. 871 64

A novel antifungal protein with its N-terminal sequence bearing similarity to the C-terminal sequences of peroxidases was isolated from French bean legumes. The protein, which possessed a molecular weight of 37 kDa, was adsorbed on Affi-gel blue gel and CM-Sepharose. The protein exhibited peroxidase activity with a Km of 58 microM and a Vmax of 3.36 U/nmol. Optimal peroxidase activity was found at 22 degrees C and pH 4. It exerted antifungal activity against a variety of fungal species including Coprinus comatus, Mycosphaerella arachidicola, Fusarium oxysporum and Botrytis cinerea. It inhibited the activities of alpha-glucosidase and beta-glucosidase but was without any inhibitory effect on HIV-1 reverse transcriptase.
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PMID:Isolation of a novel peroxidase from French bean legumes and first demonstration of antifungal activity of a non-milk peroxidase. 1213 13

A regulative two-component system previously identified in Pseudoalteromonas haloplanktis TAC125 was used to construct a cold inducible expression system that is under the control of l-malate. Performances of the inducible system were tested for both psychrophilic and mesophilic protein production using two "difficult" proteins as control. The results obtained demonstrated that both psychrophilic beta-galactosidase and yeast alpha-glucosidase are produced in a fully soluble and catalytically competent form. Optimal conditions for protein production, including growth temperature, growth medium and l-malate concentration were also investigated. Under optimized conditions yields of 620 and 27 mg/l were obtained for beta-galactosidase and alpha-glucosidase, respectively.
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PMID:An effective cold inducible expression system developed in Pseudoalteromonas haloplanktis TAC125. 1695 51

The basidiomycetous fungus Pseudozyma flocculosa represents a promising new host for the expression of complex recombinant proteins. Two novel heterologous promoter sequences, the Ustilago maydis glyceraldehyde-3-phosphate dehydrogenase (GPD) and Pseudozyma tsukubaensis alpha-glucosidase promoters, were tested for their ability to provide expression in P. flocculosa. In liquid medium, these two promoters produced lower levels of intracellular green fluorescent protein (GFP) as compared to the U. maydis hsp70 promoter. However, GPD and alpha-glucosidase sequences behaved as constitutive promoters whereas the hsp70 promoter appeared to be morphology-dependent. When using the hsp70 promoter, the expression of GFP increased proportionally to the concentration of hygromycin in the culture medium, indicating possible induction of the promoter by the antibiotic. Optimal solid-state culture conditions were designed for high throughput screening of hygromycin-resistant transformants with the hsp70 promoter in P. flocculosa.
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PMID:Usefulness of heterologous promoters in the Pseudozyma flocculosa gene expression system. 1825 90

This article presents the activity of carbohydratases and proteases in the midgut of Cameraria ohridella larvae--an oligophagous pest whose preferred feeding is horse chestnuts leaves. Optimal media pH of the assayed enzymes were similar to those of other Lepidopterans. Relatively high amylase activity, as well as maltase and sucrase activities, indicates that starch and sucrose are the main digested saccharides. Trehalase activity was similar to that described in other Lepidopterans. Activities of glycosidases were significantly lower than those of disaccharidases what suggests that neither cellulose nor glycosides are important for C. ohridella. Trypsin is the main endoprotease of this pest. Like in other leaf-eaters carboxypeptidase activity was higher than that of aminopeptidase. The activity of the majority of examined enzymes increased in the following successive pest generations, which could be explained by the decreased nutritional value of older leaves. Probably this phenomenon in hydrolases activity in Cameraria is a nonspecific mechanism present at this stage of co-evolution of the horse chestnut and its pest.
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PMID:Digestive enzymes activity in larvae of Cameraria ohridella (Lepidoptera: Gracillariidae). 2096 42