Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

This study identified and characterized hydrolytic enzymes in salivary gland products of Oestrus ovis larvae. Third instars were collected from the heads of slaughtered goats. Salivary glands were extracted, their products obtained by centrifugation and the enzymatic profile determined. Optimum pH, temperature of maximum proteolytic activity, thermal stability, and resistance of salivary gland products were determined on collagen and subclasses of proteases were identified using protease inhibitors. Zymograms were used to determine the molecular weight of proteases. Antigenic protein bands were revealed by immunoblotting using sera obtained from experimentally infested goats. Seven positive enzymatic activities were detected in salivary gland products: acid phosphatase, naphthol-AS-BI-phosphohydrolase, esterase (C4), esterase lipase (C8), leucine arylamidase, alpha-glucosidase and N-acetyl-beta-glucosaminidase. Optimum pH for proteolytic activity was 8.0; proteolytic activity increased with temperature (10-50 degrees C) then drastically decreased at 60 degrees C. Proteases in O. ovis salivary gland products belong to the serine subclass. In Zymograms, bands of proteolytic activity were detected in the 20-63 kDa range; the immunoblot showed three antigenic bands, one of them related to a protease band (63 kDa). Serine proteases in O. ovis salivary gland products are most likely involved in larval nutrition and host immuno-modulation.
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PMID:Proteolytic activity in salivary gland products of sheep bot fly (Oestrus ovis) larvae. 1769 51

Fibroblast and macrophage are 2 dominant cell types respond cooperatively to degrade implanted biomaterials. Using an electrospun Dextran/Poly-lactide-co-glycolide (PLGA) scaffold as a model, an in vitro fibroblast/macrophage co-culture system was developed to investigate the degradability of implantable biodegradable materials. SEM showed that both fibroblasts and macrophages were able to degrade the scaffold, separately or cooperatively. Under the synergistic coordination of macrophages and fibroblasts, scaffolds showed faster degradation rate than their counterparts incubated with a single type of cells as well as in PBS or cell culture medium. Lysozyme, non-specific esterase (NSE), gelatinase, hyaluronidase-1 and alpha-glucosidase were up-regulated in the presence of the scaffold, suggesting their roles in the cell-mediated scaffold degradation. In addition, the expressions of cell surface receptors CD204 and Toll like receptor 4 (TLR4) were elevated 1 week after cell seeding, implying that these receptors might be involved in scaffold degradation. The results of in vivo subdermal implantation of the scaffold further confirmed the biodegradability of the Dextran/PLGA scaffold. The fibroblast/macrophage co-culture model adequately mimicked the in vivo environment and could be further developed into an in vitro tool for initial biomaterial evaluation.
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PMID:The biodegradability of electrospun Dextran/PLGA scaffold in a fibroblast/macrophage co-culture. 1819 3

Two luminous marine bacterial strains, LC2-005(T) and LC2-102, were isolated from seawater at Kuroshio Region and Sagami Bay in Japan, respectively. These bacteria were Gram-negative, oxidase-positive, catalase-positive, motile and rod-shaped. On the basis of 16S rRNA gene sequence analysis, strains LC2-005(T) and LC2-102 formed a cluster within the Vibrio harveyi species group. However, multilocus sequence analysis using five loci (pyrH, ftsZ, mreB, gyrB and gapA) and DNA-DNA hybridization experiments indicated that these strains were distinct from the currently known Vibrio species. Additionally, these strains differ from related Vibrio species in utilization of glucose, mannitol, inositol, sorbitol, rhamnose, sucrose, melibiose and arabinose, production of lysine decarboxylase, ornithine decarboxylase, tryptophan deaminase, esterase (C4), lipase (C4), chymotrypsin, acid phosphatase, alpha-glucosidase, beta-glucosidase and N-acetyl-beta-glucosaminidase and the ability to reduce nitrate to nitrite. The major fatty acids were C(15 : 0) iso 2-OH and/or C(16 : 1)omega7c, C(16 : 0), C(18 : 1)omega7c and C(14 : 0). The DNA G+C contents of strains LC2-005(T) and LC2-102 were 45.2 and 45.5 mol%, respectively. On the basis of the polyphasic taxonomic evidence presented in this study, it can be concluded that strains LC2-005(T) and LC2-102 belong to the same genospecies and represent a novel species of the genus Vibrio, for which the name Vibrio azureus sp. nov. is proposed. The type strain is LC2-005(T) (=NBRC 104587(T) =KCTC 22352(T)).
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PMID:Vibrio azureus sp. nov., a luminous marine bacterium isolated from seawater. 1954 36

An rpoB sequence-based evaluation of 100 Mycobacterium avium complex (MAC) clinical isolates led to the identification of five respiratory tract isolates that were potential representatives of three novel MAC species. Distinctive phenotypic features of isolates 62863 and 5356591(T) included a pseudomycelium morphology and both esterase and acid phosphatase activities. These two isolates exhibited sequence similarities of 99.8 % for the 16S rRNA gene, 86.3 and 86.1 % for 16S-23S rRNA gene internal transcribed spacer (ITS-1) sequence, 96.7 and 97.8 % for rpoB and 97.6 and 97.4 % for hsp65, respectively, with the type strain of Mycobacterium chimaera, the most closely related species. Isolates 3256799 and 5351974(T) lacked alpha-mannosidase and beta-glucosidase activities. They exhibited sequence similarities of 99.6 % for the 16S rRNA gene, 90.1 and 90.4 % for ITS-1, 97.8 % for rpoB and 98.0 and 98.1 % for hsp65, respectively, with the type strain of M. chimaera, the most closely related species. Isolate 4355387(T) lacked urease and alpha-glucosidase activities, but it exhibited valine arylamidase, cystine arylamidase and acid phosphatase activities. It had sequence similarities of 99.3 % for the 16S rRNA gene, 51.8 % for ITS-1, 97.1 % for rpoB and 97.8 % for hsp65 with the type strain of Mycobacterium colombiense, the most closely related species. A phylogenetic tree based on concatenated 16S rRNA gene, ITS-1, rpoB and hsp65 sequences showed the uniqueness of these five isolates as representatives of three novel species, with bootstrap values >/=95 % in all nodes. On the basis of these phenotypic and genetic characteristics, these five isolates are proposed as representatives of three novel MAC species: Mycobacterium marseillense sp. nov., with strain 5356591(T) (=CCUG 56325(T) =CIP 109828(T) =CSUR P30(T)) as the type strain; Mycobacterium timonense sp. nov., with strain 5351974(T) (=CCUG 56329(T) =CIP 109830(T) =CSUR P32(T)) as the type strain; and Mycobacterium bouchedurhonense sp. nov., with strain 4355387(T) (=CCUG 56331(T) =CIP 109827(T) =CSUR P34(T)) as the type strain.
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PMID:Mycobacterium marseillense sp. nov., Mycobacterium timonense sp. nov. and Mycobacterium bouchedurhonense sp. nov., members of the Mycobacterium avium complex. 1962 9

Pathogenicity of fungi is connected with their ability to easily penetrate the host tissues, survive in the infected host organism and use the elements of the host tissues as nutrients. Hence, the co-occurrence of pathogenic properties with the high enzymatic activity, which is manifested through the production of various enzymes including extracellular enzymes, was observed. It can be expected that it is possible to decrease fungal pathogenicity by lowering their enzymatic activity. The aim of the study was to determine the effect of nicotinamide on enzymatic activity of the fungi, which are most frequently isolated in cases of skin infection. Enzymatic activity was analysed using 15 Candida albicans, 15 Trichophyton rubrum and 15 Trichophyton mentagrophytes strains. The strains used for the study were collected from the current diagnostic material. API ZYM tests were used in diagnostic analysis. MICs of nicotinamide were determined by the macrodilution method in liquid medium. In the case of Candida strains, the presence of nicotinamide in the broth had a significant effect on the decrease of enzymatic activity (P < 0.05) of esterase (C4), esterase lipase (C-8), valin-arylamidase, acid phosphatase and alpha-glycosydase. A considerably stronger effect of nicotinamide was observed in the case of dermatophytes (P < 0.005). Its action led to a decrease in the activity of all the enzymes under study except alpha-glucosidase produced by T. rubrum strains. Thus, nicotinamide exhibited biological activity towards C. albicans, T. rubrum and Trichophyton mentagrophytes, which resulted in a decrease in the activity of enzymes produced by the fungi.
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PMID:Inhibitory effect of nicotinamide on enzymatic activity of selected fungal strains causing skin infection. 1976 90

In Echinodontium tinctorium the presence of the following enzymes was demonstrated: esterase, maltase, lactase, sucrase, raffinase, diastase, inulase, cellulase, hemicellulase, urease, rennet, and catalase.
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PMID:ENZYME ACTION IN ECHINODONTIUM TINCTORIUM ELLIS AND EVERHART. 1987 34

Circumstantial evidence is presented which indicates that Polyporus volvatus is parasitic. Cultures of Polyporus volvatus and Fomes igniarius may be obtained from the young sporophores by the tissue method. In Polyporus volvatus the presence of the following enzymes was demonstrated: esterase, maltase, lactase, sucrase, raffinase, diastase, inulase, cellulase, hemicellulase, glucosidase, rennet, and catalase. In Fomes igniarius the presence of the following enzymes was demonstrated: esterase, maltase, lactase, sucrase, raffinase, diastase, inulase, cellulase, hemicellulase, glucosidase, urease, rennet, and catalase.
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PMID:STUDIES IN WOOD DECAY : II. ENZYME ACTION IN POLYPORUS VOLVATUS PECK AND FOMES IGNIARIUS (L.) GILLET. 1987 5

The purpose of this study was to evaluate the effect of high hydrostatic pressure (HHP) on the enzyme activities in Saccharomyces cerevisiae (ATCC 16664) and Escherichia coli (ATCC 11229). Enzyme activities before and after HHP treatment were determined using an APIZYME enzyme assay kit. Thirteen active enzymes were detected in S. cerevisiae and E. coli. Pressure treatment at 448 MPa for 30s at 23 degrees C resulted in different effects on enzymes in S. cerevisiae and E. coli. HHP completely inactivated lipase, cystine arylamidase, and chymotrypsin and moderately inactivated esterase, esterase lipase, leucine arylamidase, valine arylamidase and alpha-glucosidase in S. cerevisiae. In E. coli, esterase, esterase lipase, lipase, valine arylamidase, cystine arylamidase, trypsin, alpha-glucosidase, and beta-glucuronidase were completely inactivated and leucine arylamidase and beta-galactosidase retained partial activities. Phosphoric hydrolases were not inactivated in both microorganisms. The use of the enzyme assay kit provided rapid and useful information on the microorganisms' enzymes and their sensitivity to HHP treatment in a simple manner.
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PMID:Effect of high hydrostatic pressure on the enzyme activities in Saccharomyces cerevisiae and Escherichia coli. 2021 5

The study of metabolic scaling in stream ecosystems is complicated by their openness to external resource inputs. For heterotrophic bacteria, which are a large component of stream metabolism, it may be possible to integrate the effects of resource availability and temperature on production using metabolic scaling theory and the kinetics of extracellular enzyme activity (EEA) associated with the degradation of major nutrient pools. With this goal, we analyzed previously published data on EEA and bacterial production for two rivers in northwestern Ohio, USA. The EEA data included estimates of apparent Vmax, a measure of catalytic capacity, and apparent Km, a measure of available substrate concentration, for six extracellular enzymes (alpha-glucosidase, beta-glucosidase, aminopeptidase, protease, phosphatase, and acetyl esterase). Sampling was done over an annual cycle with a temperature range of 4 31 degrees C, while EEA assays were conducted at 20 degrees C. The EEA kinetic measures were scaled to ambient stream temperature using an activation energy (Ea) of 0.5 eV (8.01 x 10(-20) J) and converted to estimates of the turnover rate (St) of their associated substrate pools. The St values associated with protein utilization, the largest substrate pool, had the strongest relationship to bacterial production (r2 = 0.49-0.52); those for carbohydrate utilization, the smallest substrate pool, had the weakest (r2= 0.09-0.15). Comparisons of apparent Ea over the annual cycle showed that the trophic basis of bacterial production switched from relatively high carbohydrate consumption in autumn and winter to relatively high protein consumption in spring and summer, corresponding to seasonal dynamics in plant litter inputs and algal production, respectively. Over the annual cycle, the summed substrate generation rate of the six enzymes was similar in magnitude and strongly correlated with bacterial production (r2 = 0.56). This approach combines effects of substrate pool size, catalytic capacity, and temperature on bacterial production and could be used to compare ecosystems along latitudinal gradients where resource, rather than temperature, effects on metabolic scaling are of greater magnitude.
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PMID:Integrating resource utilization and temperature in metabolic scaling of riverine bacterial production. 2050 77

A stable ascorbic acid derivative, 2-O-alpha-D-glucopyranosyl-L-ascorbic acid (AA-2G), exhibits vitamin C activity in vitro and in vivo after enzymatic hydrolysis to ascorbic acid. AA-2G has been approved by the Japanese Government as a quasi-drug principal ingredient in skin care and as a food additive. In order to achieve efficient action as an ascorbic acid source, a pro-vitamin C agent, on a variety of cells or tissues, we have synthesized a series of monoacyl AA-2G derivatives. Our previous studies indicate that a series of the derivatives is a readily available source of AA activity in vitro and in vivo, and suggested that intramolecular acyl migration of the derivatives might have occurred in a neutral aqueous solution. In this study, intramolecular acyl migration and enzymatic hydrolysis of a monoacyl AA-2G derivative, 6-O-dodecanoyl-2-O-alpha-D-glucopyranosyl-L-ascorbic acid (6-sDode-AA-2G), were investigated. 6-sDode-AA-2G underwent an intramolecular acyl migration to yield ca. 10% of an isomer in neutral aqueous solutions, and the acyl-migrated isomer was isolated and characterized as 5-O-dodecanoyl-2-O-alpha-D-glucopyranosyl-L-ascorbic acid (5-sDode-AA-2G). In some tissue homogenates from guinea pigs as well as in neutral aqueous solutions, 6-sDode-AA-2G underwent partial acyl migration to give 5-sDode-AA-2G. 6-sDode-AA-2G and the resulting 5-sDode-AA-2G were predominantly hydrolyzed with esterase to AA-2G and then with alpha-glucosidase to ascorbic acid in the tissue homogenates. The results will provide a further basis for its use as an ingredient in skin care, as an effective pharmacological agent and as a promising food additive.
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PMID:Intramolecular acyl migration and enzymatic hydrolysis of a novel monoacylated ascorbic acid derivative, 6-O-dodecanoyl-2-O-alpha-d-glucopyranosyl-L-ascorbic acid. 2063 86


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