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Biomedical subjects

M M Bashor

Publications and source records attributed to M M Bashor.

15 recordsLinked to original sources
PubMed1988

Comparison of an inductively coupled plasma-atomic emission spectrometry method for the determination of calcium, magnesium, sodium, potassium, copper and zinc with atomic absorption spectroscopy and flame photometry methods.

Serum calcium, magnesium, copper and zinc concentrations obtained from the analysis of 77 serum samples by inductively coupled plasma-atomic emission spectrometry (ICP-AES) are compared with the results obtained using atomic absorption spectroscopy (AAS). Similarly, serum sodium and potassium levels from the analysis of the same samples by ICP-AES are compared with the levels obtained by flame photometry. For each metal, we compare the results from both methods with a linear regression program that assumes error in both variables. The regression analysis shows that the ICP-AES method gives slightly higher calcium, copper, and zinc results and lower magnesium results than the AAS methods, and lower sodium and potassium results than the flame photometry method. Except for sodium, the correlation (r) between the results is very high (greater than or equal to 0.958), indicating that the ICP-AES results could be corrected to be equivalent to the atomic absorption or flame photometry results. The ICP-AES has the advantage of requiring less preparation and analysis time, and additional elements could be determined simultaneously in the same sample.

Blood Specimen Collection↗
PubMed1987

Purification of prealbumin from human serum.

A method is presented by which prealbumin (thyroxine-binding prealbumin; tryptophan-rich prealbumin) may be purified to homogeneity from human serum. The method involves precipitation of contaminating proteins with dilute aqueous phenol, ion-exchange chromatography on DEAE-Sephacel, and gel permeation chromatography on Sephadex G-100. The yield is 25-30%, and the prealbumin is homogeneous by polyacrylamide gel electrophoresis at pH 8.9 and pH 3.6.

Chemical Precipitation↗
PubMed1986

Evaluation of a direct fluorometric method for determination of serum retinol.

We evaluated the usefulness of a fluorometric method for determining serum retinol (Futterman et al., Invest Ophthalmol Vis Sci 1975;14:125-30) in which fluorescence (excitation 335 nm; emission 460 nm) of retinol is directly measured in unextracted, diluted serum. Using serum from 466 individual donors, we compared values so obtained with those by a "high-performance" liquid-chromatographic method. The correlation coefficient (r) was 0.74. When we compared fluorometric retinol values with retinol-binding protein values for the 466 samples, r was 0.71. About 1% of the 466 samples had markedly higher values by fluorometry than by chromatography, the result of positive interferences. For two serum pools, we obtained CVs of 1.58% (n = 57) and 1.79% (n = 57) in long-term precision studies lasting 60 days. Although the fluorometric method of Futterman et al. has not been widely adopted, we find that it is simple to perform and that results compare favorably with the chromatographic method in precision and accuracy. It is unique among commonly used serum retinol methods in that the serum need not be extracted with organic solvents.

Chromatography, High Pressure Liquid↗
PubMed1985

Loss of vitamin A in long-term stored, frozen sera.

Vitamin A (retinol) was measured by a high performance liquid chromatography (HPLC) method in human serum samples stored frozen at -20 degrees C for 2-6 yr. In 40% of the sample, both vitamin A and the internal standard, vitamin A acetate (retinyl acetate) which was added at the time of assay, were destroyed. Controlled studies of each phase of the assay showed that the vitamin A began to degrade during the extraction step immediately after ethanol was added to the serum. Vitamin E (alpha-tocopherol) and beta-carotene also degraded concurrently with vitamin A. Vitamin A may be lost because of free radical oxidation after the vitamin is released from its serum binding protein (retinol-binding protein), following the addition of ethanol to the serum sample. The loss of vitamin A is eliminated completely if ascorbic acid (0.1% w/v) is added to the ethanol before it is used in the preassay extraction.

Chromatography, High Pressure Liquid↗
PubMed1985

Stability of vitamin A in frozen sera.

We compared values for vitamin A measured in fresh sera with values obtained after storage at -20 degrees C for five to eight years. Loss of vitamin A from long-stored sera during the extraction step was eliminated by adding ascorbic acid to the extraction solvent, ethanol. Retinol-binding protein was also measured in the stored sera. Not only did vitamin A values remain stable during the years of storage, but also the correlation between concentrations of vitamin A and retinol-binding protein in the stored sera was typical of that observed with fresh sera.

Chromatography, High Pressure Liquid↗
PubMed1983

Beta-carotene determined in serum by liquid chromatography with an internal standard.

We describe a procedure for quantitative determination of beta-carotene in human serum. The 0.1-mL serum sample is precipitated with ethanol containing the internal standard, dimethyl-beta-carotene, then extracted with hexane. This extract is injected onto a reversed-phase, "high-performance" liquid-chromatography column, and the carotenes are resolved and eluted with an acetonitrile/methylene chloride isocratic solvent system. They are quantified from the peak-height ratios of their absorbance at 450 nm. About 14 min is required for each chromatogram. The procedure has excellent precision and is appropriate for routine use in analysis of large numbers of samples. The method should be particularly useful for clinical studies on the relationship of serum beta-carotene and cancer incidence in human populations.

Carotenoids↗
PubMed1979

Vitamin A status of children in Sri Lanka.

A representative country-wide rural nutrition status survey determined the extent and distribution of vitamin A deficiency in Sri Lanka in children 6 through 71 months of age. Trained paramedical personnel recorded the presence or absence of selected ophthalmological signs and symptoms associated with vitamin A deficiency in 13,450 children. The results of the country-wide clinical survey indicate that a vitamin A deficiency problem of public health importance may exist in two of 15 health areas. Serum vitamin A levels were determined on 346 survey children from two of 15 health areas and compared with clinical findings for these areas. The lowest mean serum vitamin A, 26.3 microgram/100 ml, occurred in children with clinical eye findings. A high prevalence of clinical eye findings, 34%, and the low mean serum vitamin A value, 28.2 microgram/100 ml, were found in the group of chronically undernourished children--children who are less than 90% of their expected height for age. The survey results enabled planned redirection of the distribution of vitamin A capsules to preschool children in Sri Lanka to areas shown to have the highest prevalences of ophthalmological signs and symptoms and/or the highest prevalence of chronic undernutrition.

Child Nutritional Physiological Phenomena↗
PubMed1978

Regulation of adenosine 3':5'-monophosphate efflux from animal cells.

Cyclic AMP efflux was measured following hormonal stimulation of adenylate cyclase in a variety of animal cells including C-6 rat glioma cells, WI-38 human fibroblasts, and avian erythrocytes. Using a variety inhibitors of mitochondrial function and glycolysis, a correlation was noted between cellular ATP levels and the rate of cyclic AMP efflux in all cells examined. A relationship between the efflux rate and the magnitude of the membrane potential was not observed. Pharmacological agents which inhibited cyclic AMP egress in these cells without reducing ATP levels included several prostaglandins (A greater than B greater than E greater than F) and probenecid. The characteristics of the cyclic AMP efflux system resemble those of the organic anion transport system.

Animals↗
PubMed1975

Cellular retinol-binding protein.

1. A protein which binds retinol in vitro with high affinity and specificity was detected by sucrose gradient centrifugation or by gel filtration after preincubating rat tissue cytosols with all-trans-[3H]retinol. This protein sediments in the 2 S region of sucrose gradients. Molecular size determination by gel filtration indicates a molecular weight of 16 000. 2. Competition studies revealed that only all-trans-retinol, not retinal or retinoic acid, competes for binding. The binding of radioactive retinol is reversible. 3. This protein was detected in cytosols of rat liver, lung, spleen, brain, testis, ovaries, uterus and intestinal mucosa whereas heart or gastrocnemius muscle seem to lack this protein. 4. The cellular retinol binding protein was found in fetuses as early as day 12 of the gestation period and possessed the same specificity for the ligand as the one in adult tissues. 5. This binding component was not detected in cytosols prepared from Novikoff hepatoma, ascites hepatoma AS-30D, mouse Ehrlich ascites tumor and mouse pituitary tumor cell line AtT 20. 6. The cellular retinol binding protein seems to be different from that described to be present in the serum as suggested by difference in size and by the inability of the antisera against the serum retinol binding protein to remove the cellular binding protein from the cytosol preparations.

Amniotic Fluid↗
PubMed1975

Regulation of adenosine 3' :5'-monophosphate efflux from rat glioma cells in culture*.

Rat glioma cells grown in culture secrete cyclic adenosine 3':5'-monophosphate (cyclic AMP) into the culture medium following stimulation by beta-agonistic catecholamines. Agents which reduced cellular ATP levels such as valinomycin, oligomycin, and uncouplers of oxidative phosphorylation, inhibited cyclic AMP efflux. Secretion of cyclic AMP was also prevented by prostaglandin A-1 and pharmacological agents including probenecid and papaverine. Of the latter agents, only papaverine reduced ATP levels. These results suggest that the transport of cyclic AMP across animal cell membranes is energy-dependent and subject to regulation.

Animals↗
PubMed1973

In vitro binding of retinol to rat-tissue components.

The high-speed supernatant fraction of rat liver, lung, kidney, testis, and intestinal mucosa contains a component capable of binding [(3)H]retinol in vitro when binding is analyzed by sucrose density gradient centrifugation or gel filtration. This binding component can be distinguished from one identified in rat serum. Whereas the tissue component sediments in the 2S region of sucrose gradients, the serum component sediments in the 4.6S region. Molecular weight estimations by gel filtration indicate molecular weights of 16,000 and 67,000 for the tissue and serum binding components, respectively. Unlabeled retinol, but not retinoic acid, competes for the binding of [(3)H]retinol in tissue cytosols. Competition for the binding of [(3)H]retinol by unlabeled retinal has also been observed in tissue cytosols, but may result from the in vitro reduction of retinal to retinol. Unlabeled retinol, retinal, and retinoic acid fail to compete for the binding of [(3)H]retinol in serum under the conditions used. The tissue binding component (testis) is sensitive to digestion with Pronase, but not with RNase or DNase, indicating a protein nature for this component.

Aldehydes↗