Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.49 (glucose-6-phosphate dehydrogenase)
 7,794 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

As part of a series of epidemiological and ecological studies of leishmaniasis in Jordan, we have made functional studies of four isolates from human lesions and from ear lesions of three field-collected Psammomys obesus. Primary isolates were subcultured, frozen stabilates prepared and BALB/c mouse infectivity experiments initiated. Each mouse was inoculated with 4-8 x 10(4) promastigotes into a hind footpad. Quantitative evaluation of the footpads showed enlargement three to four weeks postinoculation. Amastigotes were readily identified in smears from footpad lesions and promastigotes in culture. At 47 days, liver and spleen samples grew out promastigotes. Biochemical characterization of these seven isolates was made by isozyme analysis using cellulose acetate membrane electrophoresis of fructokinase, phosphoglucose isomerase, phosphoglucomutase, aspartate aminotransferase, malate dehydrogenase, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Reference isolates used for comparison were Leishmania major, L. tropica minor, L. donovani, L. aethiopica and L. m. mexicana. All seven Jordan isolates showed enzyme electromorphs identical to L. major, confirming our ecological/epidemiological studies that P. obesus is a major reservoir for human cutaneous leishmaniasis in Jordan.
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PMID:Cutaneous leishmaniasis in Jordan: biochemical identification of human and Psammomys obesus isolates as Leishmania major. 304 29

Glycosomes and mitochondrial vesicles from cultured promastigotes of Leishmania mexicana mexicana have been separated using isopycnic centrifugation on linear sucrose gradients. Hexokinase (EC 2.7.1.2), glucose phosphate isomerase (EC 5.3.1.9), phosphofructokinase (EC 2.7.1.11), glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), and phosphoenolpyruvate carboxykinase (EC 4.1.1.49) were recovered largely in association with glycosomes (density; 1.215 g/ml). Phosphoglycerate kinase (EC 2.7.2.3) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) had some small glycosomal activity, but were mostly recovered in the soluble fractions. Malate dehydrogenase (EC 1.1.1.37) showed a broad peak corresponding to that of the mitochondrial marker oligomycin-sensitive ATPase (EC 3.6.1.4) (density; 1.190 g/ml). Glutamate dehydrogenase (EC 1.4.1.3) and alanine aminotransferase (EC 2.6.1.2) both showed small mitochondrial peaks, but most of the activities were recovered elsewhere on the gradient and in the soluble fractions. The subcellular location of enzymes in L.m. mexicana amastigotes was investigated by following the release of soluble enzymes from digitonin-treated amastigotes. This revealed distinct cytosolic, mitochondrial, and glycosomal compartments. The findings give an insight into the organization and control of L.m. mexicana promastigote and amastigote energy metabolism.
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PMID:Leishmania mexicana: subcellular distribution of enzymes in amastigotes and promastigotes. 315 38

Six Leishmania isolates from 3 indigenous Kenyans (2 isolates from one patient) and 2 Canadian visitors in Kenya were characterized by cellulose acetate electrophoresis. The isolates were compared among themselves and with reference strains of Leishmania donovani, L. aethiopica, L. major, L. tropica, and L. arabica using 9 enzymes: malate dehydrogenase (MDH), malic enzyme (ME), phosphogluconate dehydrogenase (6PGD), glucose-6-phosphate dehydrogenase (G6PD), aspartate aminotransferase (ASAT), adenylate kinase (AK), mannose phosphate isomerase (MPI), glucose phosphate isomerase (GPI), and phosphoglucomutase (PGM). Enzyme migration patterns of isolates from the 3 indigenous Kenyans were indistinguishable from those of 2 L. tropica reference strains. The isolates from the 2 Canadians yielded migration patterns of 7 enzymes that were indistinguishable from those of 2 L. tropica reference strains. However, migration patterns of 2 enzymes, PGM and ME, differed from all migration patterns of the 10 reference strains. Balb/c mice were inoculated with stationary phase promastigotes cultured from 3 stabilates from the lesions of 2 of the Kenyan patients. The mice developed no gross pathological lesions in 6 months time. All of the study patients developed cutaneous leishmaniasis while living in or visiting districts in Central and Rift Valley Provinces, Kenya. This is the first report of human cutaneous leishmaniasis caused by L. tropica indigenous to Africa south of the Sahara.
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PMID:Indigenous human cutaneous leishmaniasis caused by Leishmania tropica in Kenya. 317 40

A procedure for the simultaneous purification to homogeneity of hexokinase, phosphoglucomutase 1 and 2, aldolase, phosphoglucose isomerase and glucose-6-phosphate dehydrogenase from human origin has been developed. Human placenta homogenate was first chromatographed on DE-52 column which retains hexokinase and glucose-6-phosphate dehydrogenase while the other enzymes are recovered in the unabsorbed protein fraction. The other steps in the purification involve Matrex gel and specific affinity chromatography for the DE-52 retained enzymes and phosphocellulose and Matrex gel chromatography for the other enzymes. All the enzymes mentioned were obtained in one week, with recoveries from 14 percent for glucose-6-phosphate dehydrogenase to 75 percent for hexokinase. Thus, the procedures utilized seem to be useful in obtaining large amounts of enzymes in a a homogeneous form from an easily available human tissue.
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PMID:Simultaneous preparation from human placenta of several enzymes of glucose metabolism. 337 5

Effect of naphthoquinone levels on the activity of enzymes involved in glycolysis and pentose phosphate cycles was studied in male rats. Under conditions of primary and secondary K-avitaminosis the enzymatic activity, limiting these cycles, (aldolase of fructose-1,6-diphosphate, glucose phosphate isomerase and glucose-6-phosphate dehydrogenase) was increased, while the mitochondrial glutamate dehydrogenase activity was decreased. As a result of metabolic transformations under conditions of K-avitaminosis (primary and secondary) concentration of DNA in the animal tissues was lowered.
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PMID:[The effect of vitamin K on the activity of glycolysis and pentose phosphate cycle enzymes]. 342 Aug 14

Two visceral Leishmania isolates from children (aged 1 1/2 and 4 years) living in El Agamy area, Alexandria, Egypt, were compared with 5 marker strains, and 2 other human isolates from Sinai and Sudan, identified on clinical and geographical grounds as cutaneous and visceral leishmaniasis respectively. Isoenzyme variations were assessed on the basis of their electrophoretic profiles on cellulose acetate membranes. The enzymes studied were glucose 6-phosphate dehydrogenase E.C.1.1.1.49, phosphoglucomutase E.C.2.7.5.1, 6-phosphogluconate dehydrogenase E.C.1.1.1.44 (6-PGD), glucose phosphate isomerase E.C.5.3.1.9, malate dehydrogenase E.C.1.1.1.37, mannose phosphate isomerase E.C.5.3.1.8 and nucleoside hydrolase E.C.3.2.2.2. The last 4 enzymes could differentiate between cutaneous and visceral strains. The Alexandria strains proved to belong to the L. donovani complex; however, their 6-PGD pattern was identical to that of L. infantum, which was different from that of the L. donovani marker strain.
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PMID:Further characterization of Leishmania isolates from children with visceral infection in Alexandria area, Egypt. 350 8

Glucose-6-phosphate dehydrogenase (EC 1.1.1.49) prepared from baker's yeast binds to immobilized Cibacron Blue F3G-A and Procion Red HE-3B. In this paper the two dyes are compared with respect to their use in the purification of this enzyme. Cibacron Blue chromatography was found useful at an early stage of purification for the removal of contaminating hexokinase, phosphoglucose isomerase and phosphoglucomutase. With Procion Red HE-3B Sepharose the NADP dependent enzymes phosphogluconate dehydrogenase and glutathione reductase are separable from glucose-6-phosphate dehydrogenase. Unlike Cibacron Blue gel chromatography, the enzyme can be specifically eluted from Procion Red HE-3B Sepharose by a NADP gradient. Other monochlorotriazine dyes like Xirone Brillant Red BHD, 4BHD, 6BHD and GHD and the dichlorotriazine dye Procion Brown MX-5BR immobilized to Sepharose have only little binding affinity to glucose-6-phosphate dehydrogenase. The binding behaviour of different immobilized triazine dyes for pre-purified and purified glucose-6-phosphate dehydrogenase is compared. In addition, the influence of the free dyes on the activity of glucose-6-phosphate dehydrogenase is studied. It is demonstrated that the results of kinetic and binding studies with the purified enzyme are not uncritically applicable for the selection of a dye as ligand for affinity chromatography during enzyme preparation.
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PMID:Interactions of immobilized and free triazine dyes with glucose-6-phosphate dehydrogenase from yeast. 351 9

Multilocus enzyme electrophoresis was adapted to the study of Haemophilus influenzae. Protein extracts from sonicated whole bacteria were subjected to starch gel electrophoresis. After staining with substrates, the position of each isoenzyme (electromorph) was registered. Each isolate was assigned an electrophoretic type (ET) by the combination of electromorphs for the enzymes stained. Twenty-seven enzymes were tested; 12 were expressed in H. influenzae. Six enzymes were selected for subsequent study: malate dehydrogenase (MDH), phenylalanylleucine peptidase (PE2), 6-phosphogluconate dehydrogenase (6PG), adenylate kinase (AK), glucose 6-phosphate dehydrogenase (G6P), and phosphoglucose isomerase (PGI). They were polymorphic and occurred in all isolates. Six electromorphs were found for PE2, G6P, and PGI, five for MDH, four for 6PG, and three for AK. PE2, G6P, and PGI contributed most of the ET resolution (48 of 49 ETs). Multilocus enzyme electrophoresis showed several advantages over previous typing techniques. An ET could be assigned to both typable and nontypable (NT) isolates. The technique was powerful in resolving differences among isolates. The 94 isolates comprised 49 ETs, five biotypes, and six capsular types and NT isolates. Strains known to be related expressed the same ET, e.g., RAB b+ and b-, ET12; Ma a+ and a-, ET1. ET variability among type b isolates was low; 26 of 28 clinical isolates expressed ET14; 2 of 28 expressed ET13 and ET15, differing from ET14 by one electromorph each. In contrast, the 47 NT isolates comprised 38 different ETs. No ETs were shared between non-type b capsulated strains and type b or NT strains. Interestingly, five NT isolates expressed the same ET as type b strains. (iv) Strains of the same capsular type but different biotypes expressed different ETs. ET determinations will thus be useful in studying the epidemiology and evolution of H. influenzae.
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PMID:Application of multilocus enzyme gel electrophoresis to Haemophilus influenzae. 352 33

Agarose gel electrophoresis was used to identify metabolic enzymes in Babesia bovis and B. bigemina. Glutamate dehydrogenase, lactate dehydrogenase, glucose phosphate isomerase, and hexokinase were identified in B. bovis- and B. bigemina-infected erythrocytes and B. bovis merozoite preparations. A specific electrophoretic mobility was observed for each enzyme. Malate dehydrogenase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and adenylate kinase were only detected in normal erythrocyte preparations. Inter-species, but not intra-species, variation was noted when comparing electrophoretograms of both species. Kinin-activating activity was not detected in B. bovis-infected erythrocyte or merozoite preparations at pH 4.2 or 7.6.
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PMID:Enzymatic characterization of Babesia bovis. 379 41

Primary breast cancers from 85 patients undergoing post-surgical adjuvant chemotherapy were analyzed for five glycolytic enzymes: lactate dehydrogenase (LDH); phosphohexose isomerase (PHI); glucose-6-phosphate dehydrogenase (G-6PD); pyruvate-kinase (PK); and 6-phospho-gluconate dehydrogenase (6-PGD). The purpose of this study was to determine whether biochemical parameters could offer a prognostic index to determine outcome of therapy. The patients were followed up to a maximum of 54 months; during this period 30 of them developed recurrent or metastatic disease. The enzyme activities were expressed by the three following reference parameters: units/g proteins, units/g tissue weight and units/mg DNA. Two methods of analysis were compared: firstly, univariate analysis using life tables; and secondly, multivariate analysis using the Cox's model, where enzyme levels were tested for each mode of expression in addition to node status, histological features, receptor and menopausal status. Life table analyses appear limited when subsets of patients were studied because the sample size tends to become too small to warrant firm conclusions. Using the Cox's model, a prognostic index 1 was proposed, including the number of involved nodes and the product of logarithms of G-6PD and 6-PGD expressed as units/mg DNA. Compared to the number of involved nodes, this index gives a slightly better discrimination of the patients at 2 yr after mastectomy.
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PMID:Tissue glycolytic enzymes in primary breast cancer patients receiving adjuvant chemotherapy. 395 56


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