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1.
Rev. méd. Chile ; 143(2): 190-196, feb. 2015. ilus, tab
Article in Spanish | LILACS | ID: lil-742570

ABSTRACT

Background: Surgery is an effective method for the management of renal hyperparathyroidism. Aim: To report the clinical presentation and results of surgical treatment of renal hyperparathyroidism. Material and Methods: Retrospective analysis of 58 patients aged 46 ± 11 years with secondary hyperparathyroidism (HPT2) and 13 patients aged 53 ± 11 years with tertiary hyperparathyroidism (HPT3), operated at a clinical hospital. Results: In 55 cases (77.4%) the indications for surgery were complications of excess parathyroid hormone (PTH) and in 16 patients (22.6%) a failure of medical treatment. Total parathyroidectomy with intraoperative measurement of PTH (PTHop) plus a forearm parathyroid autograft was performed in 54 (93.1%) patients with HPT2 and in all patients with HPT3. PTHop decreased ≥ 75% in 51 patients (88%) with HPT2 and in 9 patients (69.2%) with HPT3, respectively. Cure of the disease was achieved in 52 (89.7%) and 11 (84.6%) patients with HPT2 and 3, respectively. Median follow-up was 41 months. Five (9.6%) patients with HPT2 and two patients (18.2%) with HPT3 had a recurrence of the disease. Conclusions: In patients with renal hyperparathyroidism, the primary indication for surgery was the presence of complications of PTH excess. A drop in PTHop ≥ 75% from baseline predicts healing in 98% and 100% of cases with secondary or tertiary HPT respectively. Surgery was a safe and effective treatment in both groups.


Subject(s)
Adult , Aged , Aged, 80 and over , Female , Humans , Male , Middle Aged , Young Adult , Carbohydrate Dehydrogenases/genetics , Carotid Intima-Media Thickness , Polymorphism, Single Nucleotide , Amino Acid Sequence , Atherosclerosis/genetics , Family Health , Gene Frequency , Genetic Predisposition to Disease/genetics , Genotype , Linear Models , Molecular Sequence Data , Risk Factors , Sequence Homology, Amino Acid
2.
Braz. j. microbiol ; 43(1): 332-340, Jan.-Mar. 2012. ilus, tab
Article in English | LILACS | ID: lil-622821

ABSTRACT

The effect of inoculation of Aspergillus flavus, Fusarium verticillioides, and Penicillium sp. in Dystrophic Red Latosol (DRL) and Eutroferric Red Latosol (ERL) soils with or without glucose on the total carbohydrate content and the dehydrogenase and amylase activities was studied. The fungal growth and spore production in culture medium with and without glucose were also evaluated. A completely randomized design with factorial arrangement was used. The addition of glucose in the culture medium increased the growth rate of A. flavus and Penicillium sp. but not of F. verticillioides. The number of spores increased 1.2 for F. verticillioides and 8.2 times for A. flavus in the medium with glucose, but was reduced 3.5 times for Penicillium sp. The total carbohydrates contents reduced significantly according to first and second degree equations. The consumption of total carbohydrates by A. flavus and Penicillium sp. was higher than the control or soil inoculated with F. verticillioides. The addition of glucose to soils benefited the use of carbohydrates, probably due to the stimulation of fungal growth. Dehydrogenase activity increased between 1.5 to 1.8 times (p <0.05) in soils with glucose and inoculated with the fungi (except F. verticillioides), in relation to soil without glucose. Amylase activity increased 1.3 to 1.5 times due to the addition of glucose in the soil. Increased amylase activity was observed in the DRL soil with glucose and inoculated with A. flavus and Penicillium sp. when compared to control.


Subject(s)
Amylases/analysis , Carbohydrate Dehydrogenases/analysis , Spores, Fungal/growth & development , Mitosporic Fungi/growth & development , Enzyme Activation , Methods , Methods
3.
Mycobiology ; : 64-66, 2011.
Article in English | WPRIM | ID: wpr-729243

ABSTRACT

Most fungi possess several hydrogen peroxide-generating enzymes, glucose oxidase and pyranose oxidase. Pyranose oxidase can use glucose as its substrate to generate hydrogen peroxide. White rot fungi, which degrade diverse recalcitrant compounds, contain lignin-degrading enzymes, and lignin peroxidase and manganese peroxidase require hydrogen peroxide for their enzymatic reactions. In this study, we isolated a cDNA fragment of pyranose oxidase from Phlebia tremellosa using PCR and examined its expression under the degradation conditions of diethylphthalate (DEP). Pyranose oxidase expression was enhanced up to 30% by the addition of DEP, and this result supports the possible involvement of pyranose oxidase in the degradation of recalcitrant compounds.


Subject(s)
Humans , Carbohydrate Dehydrogenases , DNA, Complementary , Fungi , Glucose , Glucose Oxidase , Hydrogen , Hydrogen Peroxide , Lignin , Manganese , Oxidoreductases , Peroxidase , Peroxidases , Polymerase Chain Reaction , Pyrrolidines
4.
Chinese Journal of Biotechnology ; (12): 891-895, 2007.
Article in Chinese | WPRIM | ID: wpr-327928

ABSTRACT

L-sorbose/L-sorbosone dehydrogenase from Ketogulonigenium vulgare S2 can transform L-sorbose to 2-KLG, which is widely used in production of Vitamin C. In order to obtain the engineering strain producing L-sorbose/L-sorbosone dehydrogenase and simplify the fermentation technology, firstly, this enzyme was purified by the methods of ammonium sulfate precipitation, DEAE Sepharose Fast Flow and Q Sepharose High Performance. Then, the purified L-sorbose/L-sorbosone dehydrogenase was injected to rabbit to obtain antibody. Next, the genomic library of Ketogulonigenium vulgare S2 was constructed by inserting the restriction fragments of chromatosomal DNA digested with Sau3A I into cosmid pKC505 vector digested by Hpa I and Pst I, which were packed with lamda phage package protein and transferred into E. coli DH5alpha in vitro. Finally, the positive strain K719# was selected from more than 12,000 clones via Dot-ELISA. Through the test of SDS-PAGE and thin layer chromatography, the results showed that the engineering strain K719# had the same biological activity as Ketogulonigenium vulgare S2 after adding coenzyme PQQ.


Subject(s)
Carbohydrate Dehydrogenases , Genetics , Metabolism , Cloning, Molecular , Escherichia coli , Genetics , Metabolism , Genomic Library , Gluconobacter oxydans , Genetics , Sorbose , Metabolism , Sugar Acids , Metabolism , Transformation, Bacterial
5.
Ciênc. rural ; 36(4): 1201-1206, jul.-ago. 2006. ilus
Article in Portuguese | LILACS | ID: lil-432538

ABSTRACT

Pfaffia glomerata (Spreng.) Pedersen, conhecida como ginseng brasileiro, é uma planta extensivamente usada na medicina popular em decorrência de possuir propriedades fitoterápicas. Este trabalho teve como objetivo determinar a melhor combinação de concentração da sacarose (30, 45 e 60g L-1) e do nitrogênio (50, 75, 100 e 125 por cento da concentração padrão do meio MS) para a multiplicação in vitro de P. glomerata. Aos 30 dias de cultivo, verificou-se que concentrações entre 40 e 45g L-1 de sacarose e 50 por cento de N propiciaram maior crescimento em altura e número de segmentos nodais por plântula. O número de brotações foi maior na concentração de 55g L-1 de sacarose combinada com 70 por cento de N. A matéria seca de raízes, da parte aérea e do total da plântula foi maior na concentração de 45g L-1 de sacarose associada com 50 por cento de N. No geral, a redução da concentração de N para 50 por cento daquela padrão do meio MS, associada a um incremento na dose de sacarose para 45g L-1, favorece o crescimento em altura, número de segmentos nodais e brotações, bem como a produção de biomassa de P. glomerata cultivada in vitro, devido ao estímulo ao uso do carbono.


Subject(s)
Amaranthaceae , Carbohydrate Dehydrogenases , Nitrogen/administration & dosage , Panax , Sucrose
6.
Chinese Journal of Epidemiology ; (12): 1122-1125, 2003.
Article in Chinese | WPRIM | ID: wpr-246389

ABSTRACT

<p><b>OBJECTIVE</b>To analyze factors related to the virulence associated genes of Leptospires.</p><p><b>METHODS</b>Twelve putative virulence associated genes were detected by polymerase chain reaction (PCR) method in 38 reference strains, 81 field strains of Leptospira interrogans isolated from patients or animals, and 12 avirulent strains of Leptospira biflexa.</p><p><b>RESULTS</b>These putative virulent genes were widely distributed among the strains of Leptospira interrogans, but only few of them were detected in Leptospira biflexa. Gene lipL32 was detected in all strains of Leptospira interrogans. Distribution of gene lipL36 was varied significantly with detected rates from 0 to 90.91%. Gene la1608 had a positive rate of 87.50% for strains of serogroup Icterohaemorrhagiae, but was only detected in few strains of other serogroups with a range from 0 to 25.00%. Rate of detection on gene sphA was 17.65% in Leptospira interrogans, and was absent in serovar hardjo reference strain.</p><p><b>CONCLUSION</b>Results indicated that these genes might be of importance for the virulence and pathogenicity of Leptospira interrogans, while gene lipL32 might be one of the common antigens. Gene lipL36 might be involved in serogroup specificity with genetic diversity, but gene la1608 was as one of the genes with specificity for serogroup Icterohaemorrhagiae. However, serovar hadjo might hold quite different genetic characteristics when compared with the other serovars of Leptospires.</p>


Subject(s)
Bacterial Outer Membrane Proteins , Genetics , Bacterial Proteins , Genetics , Carbohydrate Dehydrogenases , Genetics , Flagellin , Genetics , Genes, Bacterial , Genetics , Hemolysin Proteins , Genetics , Leptospira , Genetics , Virulence , Lipoproteins , Genetics , Polymerase Chain Reaction , Virulence , Genetics , Virulence Factors , Genetics
9.
Arq. biol. tecnol ; 32(3): 575-87, ago. 1989. ilus, tab
Article in English | LILACS | ID: lil-74261

ABSTRACT

An inducible L-fucose dehydrogenase from the yeast-like fungus Pullularia pullulans was purified and studied. The enzyme catalyses the oxidation of L-fucose to L-fuconic acid possibly throught its unstable L-funcono-lactone. the enzyme was purified to hemogeneity by a sequence of protamine sulfate treatment, ammonium sulfate fractionation, gel filtration on Sephadex G-100, and DEAE-cellulose chromatography. This sequence resulted in an 87 fold purification. The apparent molecular weight determined by gel filtration and SDS polyacrilamide gel electrophoresis was 40 000. the dehydrogenase was NAD-especific and showed a high sugar substrate specificity. Of several D-and L-aldoses tested only L-fucose, L-galactose and-arabinose served as substrates. The maximum velocity for the reaction was at 33- and pH 10.5. Under these conditions, the Km values, and D-arabinose, respectively. The enzyme was strongly inhibited by thiol reagents, heavy metal ions, and was not particularly stable. At 4- it rapidly los activity, but remained active for two months when maintained at -20-. The enzyme has been used to quantativate L-fucose


Subject(s)
Carbohydrate Dehydrogenases/metabolism , Fungi/enzymology
10.
Salud pública Méx ; 29(3): 195-200, mayo-jun. 1987. ilus
Article in Spanish | LILACS | ID: lil-62198

ABSTRACT

En este estudio se comparó la técnica de la coaglutinación empleando un reactivo comercial (Phadebact Gonococcus Test) con la prueba de oxidación de carbohidratos para la identificación de N. gonorrhoeae. De un total de 148 cepas aisladas en medio de Thayer-Martin o gelosa chocolate, 145 se identificaron como N. gonorrhoeae, al haber cumplido con las siguientes características: ser diplococos gramnegativos, oxidasa positivos y capaces de oxidar solamente a la glucosa. Del total de gonococos se obtuvieron 143 cepas con resultado positivo para el reactivo de coaglutinación, es decir, 98.6% de concordancia. En las tres cepas identificadas bioquímicamente como N. meningitidis se obtuvieron resultados negativos. Al realizar la coaglutinación con anticuerpos monoclonales (Phadebact Monoclonal GC Test), 59 de las cepas se identificaron como pertenecientes al serogrupo WI y las 84 restantes, al serogrupo WII/III. Así, la coaglutinación constituye una prueba rápida, fácil de realizar y de alta especificidad, y una posible alternativa para la identificación del gonococo, en lugar de la prueba tradicional de oxidación de azúcares


Subject(s)
Carbohydrate Dehydrogenases , Neisseria gonorrhoeae/isolation & purification , Agglutination Tests/methods , Antibodies, Monoclonal
11.
Bulletin of the Faculty of Science-University of Alexandria. 1984; 24 (4): 24-38
in English | IMEMR | ID: emr-4117

ABSTRACT

Glucose-6-phosphate dehydrogenase [EC 1.1.1.49] has been partially purified from Nostoc muscorum by means of ammonium sulphate precipitation/ fractionation and of exclusion gel filteration/chromatography, and some of its molecular properties were determined. Glucose-6-phosphate dehydrogenase [G6PDH] of N. muscorum was found to be absolutely NADP-specific. At pH 6.8 Km values of 0.26 mM for glucose-6-phosphate and 1.2 X 10[-5] M of NADP were determined. At higher pH the enzyme behaviour was markedly changed. Transitory initial velocities at different pH values were obvious. The well known factors affecting enzyme activities, such as enzyme substrates and divalent metal concentrations, also effected markedly, the initial velocity transition from hypoactivity to hyperactivity passing through the steady state conditions. The enzyme exhibited a slow response to rapid change in ligand concentrations, a typical property of regulatory enzymes of the hysteretic type. This was apparent in a lag during enzyme assay under steady state conditions. The lag time was found to be a decreasing function to the enzyme and glucose-6-phosphate [G6P] concentration, and the lag increased with increasing NADP concentration. The results do explain the observed nysteretic transition which may be due to molecular transition such as aggregation, polymerization, or conformational changes. However, they are insufficient to explain entire the molecular properties of glucose-6-phosphate dehydrogenase and its theoritical regulatory role. These postulations and others will be revealed in the next article under preparation


Subject(s)
Carbohydrate Dehydrogenases
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