Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0040822 (tremor)
 18,428 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The majority of tumors express an isoform of the glycolytic enzyme pyruvate kinase, the type tumor M2. The isoenzyme exists in an active tetrameric and a less active dimeric form. The dimeric form is strongly overexpressed in tumor cells and this new tumor marker is thus called tumor M2-PK. This isoenzyme is released from tumor cells and is quantitatively detectable in body fluids by a sensitive enzyme-linked immunosorbent assay (ELISA). To establish the ELISA for the routine diagnostic in a clinical laboratory, the sample stability was evaluated. Therefore, blood samples were collected in different ways from healthy donors. Reproducibility of tumor M2-PK detection in EDTA-plasma was not affected by the day to day 'stress' in a clinical routine (e.g. shaking, leaving the samples at room temperature for several hours without prior centrifugation). Similar results were obtained with citrate-plasma, whereas detection in serum and heparin-plasma was only reproducible when the blood samples were centrifuged within 2 hrs after collection. It appears that lymphocytes contain small amounts of the tumor M2-PK isoenzyme. They might release tumor M2-PK in heparin-plasma and serum samples, but not in EDTA-plasma samples. The results indicated that EDTA-plasma appears to be most appropriate for the routine diagnostic of tumor M2-PK as a tumor marker.
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PMID:Quantitative detection of tumor M2-PK in serum and plasma. 1047 Feb 35

The incorporation of [1-14C]palmitic or [1-14C]oleic acid into phosphatidylcholine and the effect on blood group antigen expression were examined in human erythrocytes stored at 4 degrees C for 0-3 weeks. Blood drawn into EDTA was obtained by venepuncture from healthy volunteers. A 50% suspension of washed erythrocytes was incubated in buffer containing [1-14C]fatty acid for up to 60 min at 37 degrees C with moderate shaking. Phosphatidylcholine was extracted and analyzed for uptake of radiolabelled fatty acid and phospholipid phosphorus content. Incorporation of [1-14C]palmitic or [1-14C]oleic acid into phosphatidylcholine was reduced during storage. The mechanism for the reduction in radiolabelled fatty acid incorporation into phosphatidylcholine was a 64% (p < 0.05) reduction in membrane phospholipase A2 activity. Although human erythrocyte membranes isolated from freshly drawn blood are capable of reacylating lysophosphatidylcholine to phosphatidylcholine, with storage, a markedly different substrate preference between palmitoyl-Coenzyme A and oleoyl-Coenzyme A was observed. Lysophosphatidylcholine acyltransferase activity assayed with oleoyl-Coenzyme A was unaltered with storage. In contrast, lysophosphatidylcholine acyltransferase activity assayed with palmitoyl-Coenzyme A was elevated 5.5-fold (p < 0.05). Despite these changes, storage of erythrocytes for up to 3 weeks did not result in altered expression of the various blood group antigens investigated. We conclude that the incorporation of palmitate and oleate into phosphatidylcholine is dramatically reduced during storage of human erythrocytes. The observed differential in vitro substrate utilization suggests that distinct acyltransferases are involved in the acylation of lysophosphatidylcholine to phosphatidylcholine in human erythrocytes.
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PMID:Incorporation of fatty acids into phosphatidylcholine is reduced during storage of human erythrocytes: evidence for distinct lysophosphatidylcholine acyltransferases. 1112 52

Eighty-three isolates from different soil samples exhibited the potential for producing active extracellular phytase. The most active fungal isolate with phytase activity was identified as Penicillium simplicissimum. In shaking culture with enrichment medium, the highest extracellular phytase activity of the producing strain was 3.8 U/mL. The crude enzyme filtrate was purified to homogeneity using ultrafiltration. IEC and gel filtration chromatography. The molar mass of the purified enzyme was estimated to be 65 kDa on SDS-PAGE. The saccharide identification with periodic acid-Schiff reagent (PAS) and activity recognition by 1-naphthyl phosphate was all positive. The isoelectric point of the enzyme, as deduced by isoelectric focusing, was pH 5.8, the optimum pH and temperature being pH 4.0 and 55 degrees C, respectively. The purified enzyme revealed broad substrate specificity and was strongly inhibited by Fe2+, Fe3+ and Zn2+; however, no inhibition was found by EDTA and PMSF. Phytase activity was inhibited when 2 mmol/L of dodecasodium phytate was added and the Km for it was determined to be 813 mmol/L.
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PMID:Isolation and characterization of a novel phytase from Penicillium simplicissimum. 1127 18

Carbazole (CA) is a heterocyclic nitrogen compound contained in the crude petroleum oil and recalcitrant to removal through the refinery processes. For development of the efficient CA-degradation bioprocess, conditions for the recycle use of Sphingomonas sp. CDH-7 resting cells were examined. When the resting cells (O.D.(660) 3.3) were shaken in 50 m M K2HPO4-KH2PO4 buffer (pH 7.0) containing CA 1000 mg/L, CA 880 mg/L was degraded within 3 h, but thereafter the activity decreased markedly. However, the activity was found to be restored to the initial level after the shaking treatment for 3 h in CA-free medium solution or in the buffer containing 20 m M MgCl2. Although the CA-degradation activity of CDH-7 resting cells was lost after 3 h of shaking in the buffer containing 100 m M EDTA, it was restored through the shaking treatment for 3 h in the buffer containing 20 m M MgCl2. When CA was periodically added eight times at a concentration of 100 mg/L (0.599 m M) to the reaction mixture containing the resting cells, CA 778 mg/L (4.66 m M) was continuously degraded within 35 h by the recycle use of resting cells, with the restoration treatment after each CA-degradation reaction by the resting cells.
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PMID:Recycle use of Sphingomonas sp. CDH-7 cells for continuous degradation of carbazole in the presence of MgCl2. 1191 Apr 94

Investigations on the bioaccumulation of the platinum group metals (PGM) Pt, Pd and Rh in aquatic organisms are of growing interest in environmental research due to the increasing emission of these metals by motor vehicles with catalytic converters. Until now, nothing is known about the possible influence of complexing agents on the bioaccumulation capacity of these precious metals. According to the partition coefficient between 1-octanol and water (POW) as a measure of bioaccumulation, in this study a simple shaking method was performed in order to investigate the effects of different complexing agents (-methionine, thio urea, EDTA, humic substances, bile compounds) on the octanol solubility of the PGM. The results demonstrated a significant influence of all agents used. -Methionine and thio urea decreased the lipid solubility. In contrast, the presence of EDTA, humic substances and especially bile caused a higher transfer of metals in the octanol phase. For most complexing agents tested, the transfer of Pd to the lipid phase was significantly higher compared with Rh and Pt, except for bile acid where the highest octanol solubility was found for Pt. Recent experimental results on PGM accumulation in zebra mussels confirm a high bioaccumulation of Pd which could be predicted from the lipid solubility.
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PMID:Lipid solubility of the platinum group metals Pt, Pd and Rh in dependence on the presence of complexing agents. 1268 77

A liquid chromatography method was developed for the determination of antifungal/antimicrobial proteins Rs-AFP1 and Dm-AMP1 in sandy loam soils. The extraction of these highly basic proteins was achieved by mechanical shaking with aqueous Tris buffer pH 9 containing guanidinium thiocyanate salt (4.1 M), EDTA and nonionic polyoxyethylene 20 cetyl ether, Brij-58 detergent. The extracts were cleaned up on Oasis HLB polymer solid-phase extraction cartridges and quantified by liquid chromatography fluorescence detection based on the fluorescence properties of the tryptophan content of these proteins. The detector response was linear for 0.3-10 microg mL(-1). Procedural recoveries were tested in the range 10-100 mg kg(-1). The limit of quantification was 10 mg kg(-1 )protein in the soil sample representing the lowest validated fortification level. The antifungal proteins were found to be stable in soil extract tested up to 9 days when stored at 4 degrees C.
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PMID:Determination of antifungal proteins in soil by liquid chromatography. 1276 64

Microglia can be isolated with high purity but low yield by shaking off loosely adherent cells from mixed glial cultures. Here we describe a new technique for isolating microglia with an average yield close to 2,000,000 microglial cells/mouse pup, more than five times higher than that of the shaking method. Confluent mixed glial cultures are subjected to mild trypsinization (0.05-0.12%) in the presence of 0.2-0.5 mM EDTA and 0.5-0.8 mM Ca2+. This results in the detachment of an intact layer of cells containing virtually all the astrocytes, leaving undisturbed a population of firmly attached cells identified as >98% microglia. These almost pure microglial preparations can be kept in culture for weeks and show proliferation and phagocytosis. Treatment with macrophage colony-stimulating factor and lipopolysaccharide, alone or in the presence of interferon gamma, induces typical microglial responses in terms of proliferation, morphological changes, nuclear factor-kappaB translocation, NO, and tumor necrosis alpha release and phagocytosis. This method allows for the preparation of highly enriched mouse or rat microglial cultures with ease and reproducibility. Because of its high yield, it can be especially convenient when high amounts of microglial protein/mRNA are required or in cases in which the starting material is limited, such as microglial cultures from transgenic animals.
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PMID:High-yield isolation of murine microglia by mild trypsinization. 1460 60

The results of clinical, neuropsychological and MRI study of 21 patients with "ephedron" encephalopathy caused by intake of methcatinon ("ephedron"), a surrogate drug obtained from phenylpropanolamine-containing compounds by adding potassium permanganate, are presented. Signs of brain lesions emerged 3-14 (mean 6.8 +/- 4.9) months after the beginning of the regular drug intake. Neurological disturbances were measured using the Scale of clinical assessment of ephedron encephalopathy. In the acute stage of the disease, most patients had the combination of extrapyramidal disorders (parkinsonism, muscular dystonia, tremor, myoclonia) with pronounced postural instability, pseudobulbar syndrome, autonomic, cognitive and affective personality abnormalities of subcortical and frontal types. In 18 (86%) patients, MRI revealed a bilateral symmetric elevation of the signal from the basal ganglia on T1-weighted images, mostly from the medial segment of globus pallidus and the reticular part of substantia nigra that reflected magnesium accumulation. The spread of hyperintensive MRI changes negatively correlated with the disease duration (r = -0.6; p < 0.01), but did not depend on the drug abuse duration or its approximate total dosage, and also did not correspond to the disease severity. In follow-up, a tendency to spontaneous regress of symptoms was observed in 29% of the cases, and in 33% patients symptoms have been regressing even 4 years after stopping of methcatinon intake. The main mechanisms of "ephedron" encephalopathy development are probably related to the manganese accumulation in the brain that might trigger secondary pathogenetic mechanisms, such as mitochondrial dysfunction, oxidative stress, etc. The induction courses of calcium and sodium EDTA that accelerates manganese excretion decrease a probability of the further disease progress, though do not contribute significantly to symptoms regress. The data on possibilities of symptomatic therapy of movement and affective disturbances is presented.
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PMID:["Ephedron" encephalopathy]. 1611 41

Extra-cellular production of a novel galactose oxidase from Fusarium acuminatum using submerged fermentation was studied. Glucose (1.0% w/v) was used as the sole carbon source. Maximum galactose oxidase production (approximately 4.0 U/ml) was obtained when fermentation was carried out at 25 degrees C, with orbital shaking (100 rpm) and an initial medium of pH 7.0, for 96 h, using a 2% (v/v) inoculum made from a homogenized four-day-old liquid culture, in the presence of copper, manganese, and magnesium. The enzyme was purified by one-step affinity chromatography, with a recovery of 42% of the initial activity. The purified enzyme ran as a single band of 66 kDa in SDS-PAGE. Optimal pH and temperature for the enzyme activity were 8.0 and 30 degrees C, respectively. The enzyme was thermoinactivated at temperatures above 60 degrees C. The purified enzyme was active toward various substrates, including galactose, dihydroxyacetone, guar gum, lactose, melibiose, methyl-galactopyranoside, and raffinose. SDS was an inhibitor but EDTA, Tween 80, NH(4)(+), Na(+), Mg(2+), K(+), and glycerol were not. The Michaelis-Menten constant (K(m)) for galactose was estimated to be 16.2 mM, while maximal velocity (V(max)) was 0.27 micromol of H(2)O(2) . ml(-1) . min(-1).
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PMID:Production, purification, and characterization of a novel galactose oxidase from Fusarium acuminatum. 1751 13

Intraepithelial leukocytes (IELs) form an important component of the intestinal immune system. Several methods of preparing chicken IELs were compared for cell yield, cell populations, and functional activity against a natural killer (NK)-susceptible lymphoblastoid cell line (LSCC-RP9). In addition, an attempt was made to immortalize IELs by infection with reticuloendotheliosis virus (REV) for use in cell-trafficking studies. Intestinal fragments were incubated in 5 mM DL-dithiothreitol at 41 degrees C for 15 min followed by three 45 min incubations in 0.1 mM EDTA. Gentle shaking of the intestinal fragments every 5 min caused considerably less damage to the epithelial cell layer than slow stirring with a magnetic bar. The latter method yielded more cells, but these were not functionally active in the NK-cell assay. The more gentle method resulted in a lower cell yield, but these cells were able to lyse LSCC-RP9; the percentage of lymphocytes present was lower but these contained a higher proportion of large granular lymphocytes. Infection of IELs with REV did not immortalize these cells.
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PMID:Preparation and characterization of chicken intraepithelial leukocytes. 1867 Oct 36


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