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Biomedical subjects

Z Zaman

Publications and source records attributed to Z Zaman.

At least 37 records · Page 2Linked to original sources
PubMed1998

Disappointing dipstick screening for urinary tract infection in hospital inpatients.

AIM: To compare the performance of leucocyte esterase and nitrite dipstick tests with microscopic examination and culture of first morning urines (n = 420) of hospital inpatients. RESULTS: The sensitivity, specificity, and negative predictive value of the leucocyte esterase test for the cutoff of > 10 WBC/microliter were 57%, 94%, and 68%, respectively. For > 5 WBC per high power field (HPF) these variables were 84%, 90%, and 93%. For > 10(5) colony counts/ml, the sensitivity of the nitrite test was 27%, specificity 94%, and negative predictive value 87%. When either leucocyte esterase or nitrite positivity was accepted as a marker of urinary tract infection, the sensitivity was 78%, specificity 75%, and negative predictive value 94%, and there were 22% false negative results. Semiquantitative microscopic estimation of bacteria per HPF yielded 40% false positives. CONCLUSIONS: Leucocyte esterase and nitrite dipstick tests are not suitable for screening for urinary tract infections.

Adolescent↗
PubMed1998

Evaluation of Glucocard Memory 2 and Accutrend sensor blood glucose meters.

The performance and practicability of 2 blood glucose meters (Glucocard Memory 2 and Accutrend sensor) were evaluated. Both glucose meters produced acceptably precise results in the hyper- and normoglycaemic concentration ranges. In the hypoglycaemic concentration range, the imprecision of Accutrend sensor was much higher than recommended by the American Diabetes Association. Within-run coefficients of variation for Glucocard Memory 2 were 6.3%, 3.9% and 2.4% at glucose concentrations of 1.7 mmol/l, 5.8 mmol/l and 11.7 mmol/l, respectively: for Accutrend sensor these were 15.2%, 5.0% and 1.2% at respective concentrations of 0.9 mmol/l, 4.2 mmol/l and 19.6 mmol/l. Between-day coefficients of variation for Glucocard Memory 2 were 4.8% and 3.5% at glucose concentrations of 3.9 mmol/l and 17.2 mmol/l, respectively and for Accutrend sensor they were 3.8% and 2.9% at glucose concentrations of 3.8 mmol/l and 18.7 mmol/l, respectively. Results were linear over a range of 1.6 mmol/l -29.7 mmol/l for Glucocard Memory 2 and 1.6 mmol/l -33.3 mmol/l for Accutrend sensor. Results of both blood glucose meters correlated closely with the hexokinase/glucose-6-phosphate dehydrogenase laboratory method. Ninety-eight percent of both Glucocard Memory 2 and Accutrend sensor results were within 20% of the comparison method values. Ninety-three percent of the Glucocard Memory 2 and 96% of the Accutrend sensor results were within 15% of the comparison method results. An inverse relation between the glucose readings and haematocrit values was observed for both blood glucose meters in the hyperglycaemic range and this effect was more pronounced for Accutrend sensor. In the normo- and hypoglycaemic ranges the effect was insignificant and absent, respectively. Minimum sample volume for Glucocard Memory 2 was 3 microliters and for Accutrend sensor it was 9 microliters. Lower sample volumes gave erroneous results. Presenting more than the required volume had no effect on results.

Analysis of Variance↗
PubMed1997

Inhibition of acetylcholine esterase and choline esterase by benzethonium chloride and avoidance of the benzethonium chloride carry-over inhibitory effect.

It has been shown that benzethonium chloride produces linear mixed-type inhibition of choline esterase and acetylcholine esterase. These enzymes also show-reagent-carry-over inhibition if the enzyme activities are measured in plastic cuvettes in which previously protein has been determined by the alkaline benzethonium chloride method. Choline esterase is about 10-fold more sensitive to benzethonium chloride than acetylcholine esterase. With acetylthiocholine as substrate Michaelis-Menten constants for choline esterase and acetylcholine esterase are 85 mumol/l and 102 mumol/l, respectively. Carry-over inhibitory effect of benzethonium chloride can be avoided by washing the cuvettes, after protein determination by the benzethonium chloride method, with 5 ml/l Triton X-100, 5 ml/l Tween 20 or 10 g/l sodium dodecyl sulphate. The latter has a disadvantage in that it precipitates out at low temperatures. The dry slide method (Johnson & Johnson) for serum choline esterase is free of the inhibitory effect until the concentration of benzethonium chloride in the sample reaches about 200 mumol/l.

Acetylcholinesterase↗
PubMed1995

Elimination of paraprotein interference in determination of plasma inorganic phosphate by ammonium molybdate method.

Phosphate concentrations were determined in 52 cases of paraproteinemia. The unmodified acidic ammonium molybdate method produced 19% spuriously high results. The false increase of phosphate concentration was attributable to formation of precipitate in the reaction mixture. The precipitate was formed by interaction between immunoglobulins and the unmodified acidic ammonium molybdate reagent. The magnitude of interference bore no relation to the type, concentrations, or isoelectric point of the paraproteins or to the presence or absence of free light chains. Diluting the sample to approximately 40 g/L total protein reduced but did not always eliminate the interference. In some cases paraprotein concentration as low as 8 g/L falsely increased plasma phosphate results. Apparently, only IgG and IgM but not IgA paraproteins produced the interference. Deproteination by ultrafiltration or by treatment with trichloroacetic acid removed the interference. The Kodak slide method and the new modified Boehringer Mannheim phosphate test were found to be interference-free. However, in some cases the latter new formulation is sensitive to substantial changes in ionic concentration of the reaction mixture.

Ammonium Sulfate↗
PubMed1994

Multiphasic modelling of ligand/acceptor interactions. The hydrophobicity-dependent binding of relatively small amphiphilic substances to acceptor proteins and the nature and facedness of acceptor sites.

The modelling of multiphasic ligand/acceptor equilibrium binding systems proceeds at three logically distinct levels: (1) A suitable response quantity, e.g. the amount of acceptor-bound ligand nEL, is expressed as a function of the ligand concentrations [Li] (L = A,B,...) in the compartment i that contains the acceptor sites. One thus obtains a response function nEL = f1([Li]). In general, the equilibrium constants KL contained in such mathematical models are physically ill-defined. (2) Each local concentration [Li] is further expressed as a function of [Laq], the corresponding concentration in the aqueous phase, leading to nEL = f2([Laq]). In this way, the constants KL are transformed into effective constants K'L which (i) can be assessed experimentally and (ii) depend on ligand hydrophobicity in a way that is characteristic of the binding site. Formulation of the functions f1 and F2 only requires knowledge of the reactions in which the acceptor sites participate directly. (3) For each ligand, the experimentally accessible total ligand concentration Lt is expressed as a function of [Laq], leading to concentration balance equations Lt = Lt([Laq]). The latter transformation takes account of any reactions, distinct from ligand/acceptor interaction, in which the ligands are involved, e.g. binding to additional protein sites. As a result of steps 2 and 3, each binding system is described by a set of simultaneous equations dependent on the auxiliary variable [Laq]: (i) the response function f2([Laq]) and (ii) a concentration balance for each ligand Lt = Lt([Laq]). The formulae are rendered more conscise and their discussion and application to data fitting are simplified by introducing, for each ligand L, a function FL characterising the distribution of unbound monomeric ligand over the various partition compartments. When the acceptor acts on unbound ligand, the formulae are further expressed in terms of a new auxiliary variable i.e. the total concentration of unbound monomeric ligand microL. In contrast to data analysis as a function of local concentrations, analysis in terms of total ligand concentrations avoids losing sight of alternate hypotheses about the nature of the binding sites. The present formulation has also permitted clarification of several consequences of the multiphasic nature of the binding systems that, as yet, have been poorly recognised.(ABSTRACT TRUNCATED AT 400 WORDS)

Binding Sites↗
PubMed1994

Simultaneous macroamylasemia and macrolipasemia.

The first case of the simultaneous presence of macroamylasemia and macrolipasemia in a patient with gluten enteropathy (celiac disease) is described. Both macroenzymes were formed by association of polyclonal IgA with amylase and lipase. Both macroenzymes had molecular masses > 300 kDa.

Amylases↗
PubMed1993

Simultaneous determination of vitamins A and E and carotenoids in plasma by reversed-phase HPLC in elderly and younger subjects.

A reversed-phase high-performance liquid-chromatographic method for the simultaneous determination of retinol, alpha-tocopherol, alpha-carotene, beta-carotene, cryptoxanthin, lutein/zeaxanthin, and lycopene is described. This method was applied to plasma measurements in healthy young and elderly subjects. The plasma, deproteinized with ethanol, is extracted twice with n-hexane. After evaporation, the residue is dissolved in 50 microL of tetrahydrofuran and made up to 200 microL with ethanol. Samples (50 microL) are injected onto a 250 x 4.6 mm column of 5-microns-particle Spherisorb ODS1 (Phase Separations) that had been equilibrated with solvent mixture A:B (90:10 by vol) [A = 100 mmol/L ammonium acetate in methanol: acetonitrile (80:20 by vol) and B = 100 mmol/L ammonium acetate in water] at 2 mL/min. The analytes are eluted by running a 12-min linear gradient to 100% A; solvent A is then maintained for 10 min. Intrabatch CVs were 2.3%, 3.3%, 2.8%, 3.6%, 3.6%, and 3.0% for retinol, alpha-tocopherol, lutein/zeaxanthin, cryptoxanthin, lycopene, and beta-carotene, respectively. The corresponding interbatch CVs were 4.9%, 5.8%, 12.3%, 6.5%, 8.0%, and 3.4%.

Adult↗
PubMed1992

Positive regulation of the LPD1 gene of Saccharomyces cerevisiae by the HAP2/HAP3/HAP4 activation system.

The LPD1 gene of Saccharomyces cerevisiae, encoding lipoamide dehydrogenase (LPDH), is subject to catabolite repression. The promoter of this gene contains a number of motifs for DNA-binding transcriptional activators, including three which show strong sequence homology to the core HAP2/HAP3/HAP4 binding motif. Here we report that transcription of LPD1 requires HAP2, HAP3 and HAP4 for release from glucose repression. In the wild-type strain, specific activity of LPDH was increased 12-fold by growth on lactate, 10-fold on glycerol and four- to five-fold on galactose or raffinose, compared to growth on glucose. In hap2, hap3 and hap4 null mutants, the specific activities of LPDH in cultures grown on galactose and raffinose showed only slight induction above the basal level on glucose medium. Similar results were obtained upon assaying for beta-galactosidase production in wild-type, or hap2, hap3 or hap4 mutant strains carrying a single copy of the LPD1 promoter fused in frame to the lacZ gene of Escherichia coli and integrated at the URA3 locus. Transcript analysis in wild-type and hap2 mutants confirmed that the HAP2 protein regulates LPD1 expression at the level of transcription in the same way as it does for the CYC1 gene. Site-directed mutagenesis of the putative HAP2/HAP3/HAP4 binding site at -204 relative to the ATG start codon showed that this element was required for full derepression of the LPD1 gene on non-fermentable substrates.

Base Sequence↗
PubMed1992

Plasma concentrations of vitamins A and E and carotenoids in Alzheimer's disease.

In a case/control study, serum concentrations of vitamins A and E and major carotenoids were determined in patients with Alzheimer's disease, multi-infarct dementia and control subjects. The results showed that both Alzheimer's and multi-infarct dementia patients had significantly lower levels of vitamin E and beta-carotene than controls (vitamin E: 18.65 +/- 3.62 mumol/l in Alzheimer's disease and 15.80 +/- 6.93 mumol/l in multi-infarct dementia versus 30.03 +/- 12.03 mumol/l in controls; beta-carotene less than 0.13 to 0.42 mumol/l in Alzheimer's disease and less than 0.13 to 0.30 mumol/l in multi-infarct dementia versus 0.13 to 1.53 mumol/l in controls). Vitamin A was significantly reduced only in the Alzheimer's patients (1.56 +/- 0.78 mumol/l in Alzheimer's disease versus 2.13 +/- 0.86 mumol/l in controls).

Aged↗
PubMed1992

A 3' transcriptional enhancer within the coding sequence of a yeast gene encoding the common subunit of two multi-enzyme complexes.

A well-defined set of isogenic yeast strains has been constructed whereby each strain contains a different LPD::lacZ gene fusion integrated at the ura3 locus. These LPD::lacZ fusions differ in the amount of the LPD1 gene (encoding lipoamide dehydrogenase) that is fused to the lacZ reporter. Comparison of the beta-galactosidase activities of each strain during growth on glucose or ethanol revealed that some part of the LPD1 coding region between +13 and +700 is involved in activating gene expression in a carbon source-dependent manner. This activation occurs at the mRNA level, and is not mediated by changes in mRNA stability. Therefore, the LPD1 gene appears to contain a transcriptional enhancer that lies 3' to the transcriptional start site, and which responds to carbon source.

Base Sequence↗
PubMed1987

Effect of acute lead intoxication on the ultrastructure of rat erythroblasts and reticulocytes. Morphometric analysis and röntgen micro-analysis.

Effect of 17 hr intoxication of lead on the different maturation stages of erythroid cells were studied in rat. Morphometric methods were used to analyse the lead-induced ultrastructural changes in the early, intermediate, late erythroblasts and reticulocytes. It was found that the toxic effect of lead increases with maturation. Energy-dispersive Röntgen micro-analysis showed that fibrillar structures within vesicles and endoplasmic reticulum contained lead.

Acute Disease↗
PubMed1981

Non-enzymic glycosylation of horse spleen and rat liver ferritins.

Incubation of horse spleen ferritin and rat liver ferritin with [14C]glucose, [14C]mannose or [14C]fucose resulted in the covalent incorporation of the sugar into ferritin. The rate of reaction depended on the concentrations of ferritin and sugar and time of incubation. The order of this nonenzymic incorporation was glucose greater than mannose greater than or equal to fucose. Glucosylated or mannosylated ferritin was not retained by concanavalin A. The plasma half-life of rat liver ferritin and apoferritin was found to be 20 min. This value remained unaffected by in vitro glucosylation or mannosylation of ferritin. It is suggested that varying degrees of glycosylation might account for the occurrence of isoferritins.

Animals↗
PubMed1981

Influence of zinc on iron uptake by monolayer cultures of rat hepatocytes and the hepatocellular ferritin.

Monolayer cultures of isolated rat hepatocytes on collagen gels were used to study the effect of zinc on (a) 59Fe uptake by the hepatocytes; (b) 59Fe uptake by the hepatocellular ferritin and (c) biosynthesis of ferritin and total proteins. While deposition of iron into the cellular ferritin was inhibited by zinc in a dose-dependent manner, iron uptake by the hepatocytes was inhibited significantly only at high concentrations of zinc. Biosynthesis of total proteins or ferritin was not affected by zinc. Since only a small fraction of the cellular 65Zn was found to be associated with ferritin, it was concluded that zinc was not deposited in ferritin. Intracellular distribution of 59Fe revealed that newly accumulated iron went into an iron pool the size of which could be increased by the presence of zinc.

Animals↗
PubMed1980

Studies on the mechanism of transferrin iron uptake by rat reticulocytes.

Mechanism of transferrin iron uptake by rat reticulocytes was studied using 59Fe- and 125I-labelled rat transferrin. Whereas more than 80% of the reticulocyte-bound 59Fe was located in the cytoplasmic fraction, only 25-30% of 125I-labelled transferrin was found inside the cells. As shown by the presence of acetylcholine esterase, 10-15% of the cytoplasmic 125I-labelled transferrin might have been derived from the contamination of this fraction by the plasma membrane fragments. Electron microscopic autoradiography indicated 26% of the cell-bound 125I-labelled transferrin to be inside the reticulocytes. Both the electron microscopic and biochemical studies showed that the rat reticulocytes endocytosed their plasma membrane independently of transferrin. Sepharose-linked transferrin was found to be capable of delivering 59Fe to the reticulocytes. Our results suggest that penetration of the cell membrane by transferrin is not necessary for the delivery of iron and that, although it might make a contribution to the cellular iron uptake, internalization of transferrin reflects endocytotic activity of the reticulocyte cell membrane.

Acetylcholinesterase↗
PubMed1977

Comparison of the biliary excretion of the four isomers of bilirubin-IX in Wistar and homozygous Gunn rats.

The biliary excretion of the four isomers of bilirubin-IX was studied in Wistar rats (JJ) and homozygous Gunn rats (jj). Synthetic preparations of 14C-labelled pigments were used. 1. After intravenous administration, the alpha-isomer was rapidly excreted in conjugated form in bile of Wistar rats. In Gunn rats excretion was insignificant. In contrast, both rat species promptly excreted the non-alpha-isomers at rates that were comparable with that found for bilirubin-IXalpha in Wistar rats. 2. In normal rats about 16% of the beta- and delta-isomers and at least 50% of the gamma-isomer were excreted as ester conjugates of the injected parent bile pigments. Conjugation of the beta- and delta-isomers had occurred exclusively at the carboxyl groups of pyrrole ring D and C respectively. For bilirubin-IXgamma no preference for any carboxyl group could be established. 3. In homozygous Gunn rats the non-alpha-isomers were apparently excreted chemically unaltered. This suggests that, as for bilirubin-IXalpha, conjugation of the non-alpha-isomers is also deficient in Gunn rats.

Animals↗