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At least 1,693 records · Page 94Linked to original sources
PubMed1975

Preparation and partial characterization of hepatic regenerative stimulator substance (SS) from rat liver.

1. The elucidation of the biochemical controls of growth processes is basic to understanding both normal and malignant growth. The exquisitely sensitive control demonstrated in the regenerating liver provides an excellent model system for growth studies. 2. Intraperitoneal injection of an extract from weanling rat liver into 34% hepatectomized rats stimulates [3H]thymidine incorporation into recipient hepatic DNA 2.5-fold. This stimulation is seen after a 10 hr lag period. 3. Extracts from weanling rat liver contain the highest level of the hepatic regenerative stimulator substance (SS), whereas extracts from adult liver give no significant stimulation. 4. If adult rats are partially hepatectomized, SS is demonstrated in their livers 12-15 hr after hepatectomy. 5. Partial characterization of SS shows that it is a soluble material not sedimented by centrifugation for 2 hr at 145,000 g. The stimulator activity is stable to heating at 65 degrees C and 100 degrees C for 15 min but is lost when treated with 10% perchloric acid.

Age Factors↗
PubMed1972

Separation of skin reactive intestinal cancer antigen from the carcinoembryonic antigen of Gold.

Soluble fractions of human intestinal cancer and fetal intestinal cell membranes produced delayed hypersensitivity reactions in patients with intestinal cancer. These soluble fractions and perchloric acid extracts of intestinal cancer cells were fractionated by polacrylamide-gel electrophoresis. The Gold carcinoembryonic antigen was found in a region of the gels different from that of the skin reactive antigen.

Antigens↗
PubMed1982

Interspecies variations in mammalian lens metabolites as detected by phosphorus-31 nuclear magnetic resonance.

Multiple interspecies differences were detected between humans and seven other mammals in 15 of the 24 metabolites measured in the intact crystalline lens and lens perchloric acid extracts. Generally, the number of statistically significant metabolite differences among the various species, relative to the human, increase in the following order: cat or approximately dog greater than pig greater than rat greater than sheep greater than rabbit greater than cow.

Adenine Nucleotides↗
PubMed1981

Liquid chromatographic assay for metronidazole and tinidazole: pharmacokinetic and metabolic studies in human subjects.

We developed methods for measuring metronidazole, its two major metabolites, and tinidazole in serum and urine. After treatment of each sample with an equal volume of 5% perchloric acid, the drugs were separated by reverse-phase high-pressure liquid chromatography (retention times, 6 to 18 min). Quantitation was based on spectrometry at 320 nm. These assays were sensitive, rapid, and specific, and recoveries from biological samples were quantitative. Metronidazole and tinidazole were given as rapid intravenous infusions to four healthy human volunteers. The biological half-lives of these two compounds were 5.4 and 11.1 h, respectively. The hydroxy metabolite of metronidazole appeared quickly in serum and was eliminated at a slow rate. The acetic acid metabolite of metronidazole was detected in serum at very low levels and only for a limited time. No metabolic products of tinidazole were found in serum samples. In urine, 43.7% of the administered dose of metronidazole was recovered over a period of 24 h (24.1% of the dose as the hydroxy metabolite, 12.0% as the acetic acid metabolite, and 7.6% as unchanged drug). Only 18.4% of the infused dose of tinidazole was eliminated in urine over a period of 72 h, and no metabolic products were detected.

Chromatography, High Pressure Liquid↗
PubMed1983

Determination of ceftazidime in biological fluids by using high-pressure liquid chromatography.

Ceftazidime is a new beta-lactamase-stable third-generation cephalosporin with a broad spectrum of antimicrobial activity. To evaluate the biodisposition of the drug in infants and children, a rapid and simple high-pressure liquid chromatographic technique was developed. The method is useful for both serum and urine and involves methanol precipitation followed by reverse-phase chromatography on MicroPak MCH 10. The mobile phase, consisting of 20% methanol and an 80% aqueous solution of 50 mM ammonium dihydrogen phosphate and 117 microM perchloric acid, is pumped at 1 ml/min through the column which is maintained at 50 degrees C. The drug was detected at 257 nm with a variable-wavelength UV detector. A good linear correlation was observed between the peak area and the ceftazidime concentration at 0.3 to 500 micrograms/ml (r = 0.999). Since an equal volume of cold methanol is used to precipitate proteins from serum samples and only 20 microliters of the resultant supernatant is injected into the column, samples as small as 50 microliters may be routinely analyzed. This method has been used to study ceftazidime pharmacokinetics in more than 30 patients and has proven to be rapid and reproducible.

Ceftazidime↗
PubMed1985

Rapid method for determination of kanamycin and dibekacin in serum by use of high-pressure liquid chromatography.

A rapid, simple, and accurate method for the determination of kanamycin and dibekacin in serum by use of high-pressure liquid chromatography is described. The serum proteins were precipitated with 3.5% perchloric acid containing sodium octanesulfonate. After centrifugation, a sample of the supernatant was directly injected into the chromatograph. The determination of kanamycin and dibekacin was performed by a combination of reverse-phase, ion-pair chromatography, postcolumn derivatization with o-phthalaldehyde, and fluorescence detection. The correlation coefficients with fluorescence polarization immunoassay were 0.996 for kanamycin and 0.957 for dibekacin.

Chromatography, High Pressure Liquid↗
PubMed1983

Detection of T-2 toxin by an improved radioimmunoassay.

T-2 toxin in serum, urine, and saline was analyzed by a modified radioimmunoassay procedure. The specimens were added directly to the assay tubes without extraction steps. The reaction between antibody and ligands was optimal at 1 h. Albumin-coated charcoal was used to separate bound from free radioactivity. Quenching, which occurred with hemolyzed specimens, was corrected by a wet oxidation process with 60% perchloric acid and 30% hydrogen peroxide. The shorter incubation times resulted in an assay that takes less than 6 h to complete. The average affinity constant of the antibody (Km) was 1.75 X 10(10) liters/mol. The sensitivity was 1 ng per assay or 10 ng/ml. Among the other trichothecenes tested, only H-T-2 cross-reacted significantly (10.3%).

Antibody Affinity↗
PubMed1989

Efficacy of phospholipid analysis in determining microbial biomass in sediments.

Improvements in the analysis of lipid-bound phosphates resulted in a simplified and sensitive method for determining microbial biomass in sediments. Sensitivity was enhanced over previous methods by use of a dye, malachite green, which when complexed with phosphomolybdate at low pH has a high extinction coefficient (at 610 nm). The use of a persulfate oxidation technique to liberate phosphate from lipids increased the simplicity and safety of the method relative to the traditional perchloric acid digestions. The modified method was both accurate (yielding quantitative recoveries of cells added to sediments) and precise (coefficient of variation of less than 5% for cells and sediments). A comparison with an epifluorescence technique indicated that the analysis of lipid-bound phosphate was more rapid and less tedious and could be successfully applied to a wider variety of sediment types. An estimate of the lipid-bound phosphate-to-carbon conversion factor based on a diverse enrichment culture from sediments suggested that previous factors for pure cultures may have been too low.

Journal Article↗
PubMed2002

Identification of opuC as a chill-activated and osmotically activated carnitine transporter in Listeria monocytogenes.

The food-borne pathogen Listeria monocytogenes is notable for its ability to grow under osmotic stress and at low temperatures. It is known to accumulate the compatible solutes glycine betaine and carnitine from the medium in response to osmotic or chill stress, and this accumulation confers tolerance to these stresses. Two permeases that transport glycine betaine have been identified, both of which are activated by hyperosmotic stress and one of which is activated by low temperature. An osmotically activated transporter for carnitine, OpuC, has also been identified. We have isolated a Tn917-LTV3 insertional mutant that could not be rescued from hyperosmotic stress by exogenous carnitine. The mutant, LTS4a, grew indistinguishably from a control strain (DP-L1044) in the absence of stress or in the absence of carnitine, but DP-L1044 grew substantially faster under osmotic or chill stress in the presence of carnitine. LTS4a was found to be strongly impaired in KCl-activated as well as chill-activated carnitine transport. 13C nuclear magnetic resonance spectroscopy of perchloric acid extracts showed that accumulation of carnitine by LTS4a was negligible under all conditions tested. Direct sequencing of LTS4a genomic DNA with a primer based on Tn917-LTV3 yielded a 487-bp sequence, which allowed us to determine that the opuC operon had been interrupted by the transposon. It can be concluded that opuC encodes a carnitine transporter that can be activated by either hyperosmotic stress or chill and that the transport system plays a significant role in the tolerance of L. monocytogenes to both forms of environmental stress.

ATP-Binding Cassette Transporters↗
PubMed1970

Volutin granules in Zoogloea ramigera.

Zoogloea ramigera, a gram-negative bacterium found in activated sludge, formed volutin granules when excess orthophosphate was added to a phosphate-starved culture. These volutin granules were stainable by hydrogen sulfide after lead acetate treatment and extractable by N-perchloric acid but were not adsorbed by activated charcoal. They appeared to consist of inorganic polyphosphate. Optimum granule formation in the arginine broth required 10 g of glucose, 3 mg of phosphate, and 1 to 20 mg of magnesium per liter of medium. At an Mg(2+) concentration of 1 mg/liter, very large granules appeared which often appeared to fill the cell. An excess of glucose, orthophosphate, or magnesium reduced granule formation. In the absence of sulfate, moderate granulation occurred in arginine broth before the addition of excess orthophosphate; granulation did not increase after the addition of phosphate.

Arginine↗
PubMed1977

Reproduction of the eosinopenia of acute infection by passive transfer of a material obtained from inflammatory exudate.

Studies of the eosinopenic effect of acute inflammation were conducted in mice previously rendered eosinophilic with trichinosis. Exudate removed from a pneumococcal abscess contained material (eosinopenic factor [EF]) capable of causing eosinopenia of 4- to 24-h duration when injected intraperitoneally into eosinophilic mice. The material passed through a 0.45-micronm filter, but was retained by a dialysis membrane capable of retaining protein molecules of greater than approximately 30,000 molecular weight. EF was soluble in 7% perchloric acid, was not destroyed by pneumococcal proteolytic enzymes in the presence of Trasylol, but was inactivated by heating to 56 degrees C for 30 min. EF was detectable in the exudate after 10 h and had reached its highest concentration after 20 h. When the effect of EF was expressed as a percent suppression of control eosinophil levels, there was a geometric dose response. Eosinopenia could not be ascribed to steroids present in the preparation, and the EF was effective in adrenalectomized animals. Eosinopenia was not induced by transfer of similarly treated heat-killed pneumococci, pneumococcal culture filtrate, or normal serum. The eosinopenia of acute infection may be the direct effect of a substance present at the site of acute inflammation.

Adrenalectomy↗
PubMed1986

Clearance of endotoxin from blood of rabbits injected with staphylococcal toxic shock syndrome toxin-1.

This study was undertaken to examine some of the properties of staphylococcal toxic shock syndrome toxin 1 (TSST-1) with regard to the clearance of endotoxin from blood. The concentration of endotoxin in blood was measured by using a chromogenic limulus test and modified perchloric acid method. When TSST-1, which produces fever in rabbits, was injected (100 ng/ml or 100 micrograms/ml per kg) intravenously (i.v.) into the animals, no measurable level of endotoxin was detected in the blood. In control animals, which were given 5 micrograms of endotoxin per ml per kg i.v., endotoxin could be detected in the blood at rapidly declining levels. These results suggested that TSST-1 might not lead bacterial endotoxin from other body sites into the blood. When the animals were given TSST-1 (1 to 100 ng/ml per kg) i.v. and then endotoxin (5 micrograms/ml per kg) i.v. 4 h later, endotoxin was detected in the blood at a high level, depending on the dose of TSST-1 injected. These results showed that TSST-1 inhibited the clearance of endotoxin in the blood; this clearance is thought to be mainly done by the reticuloendothelial system. In the animals given TSST-1 (100 ng/ml per kg) and endotoxin (5 micrograms/ml per kg) simultaneously, the endotoxin level in the blood was found to be higher than that in control animals given endotoxin only but lower than that in the animals given TSST-1 and then endotoxin at the same doses.

Animals↗
PubMed1974

5-Bromouridylyl-(3-5)-adenosine isolated from 5-bromouracil-induced filaments of Escherichia coli.

A dinucleoside monophosphate was isolated from 5-bromouracil-induced filaments of a thymine auxotroph of Escherichia coli K-12. The dinucleoside monophosphate was fractioned from a [(14)C]5-bromouracil-labeled perchloric acid extract using Dowex-1-formate ion-exchange chromatography. Sephadex chromatography revealed its molecular weight to be 710. Snake venom phosphodiesterase digest of the dinucleoside monophosphate yielded [(14)C]5-bromouridine and adenosine 5'-monophosphate. The presence of [(14)C]5-bromouracil in bacterial ribonucleic acid indicates that ribonucleic acid, which had incorporated 5-bromouracil, was the probable source of this dinucleoside monophosphate, 5-bromouridylyl-(3' --> 5')-adenosine.

Adenosine↗
PubMed1980

Inhibition and activation of mannan synthesis in Saccharomyces cerevisiae spheroplast lysates.

Mannan synthetase activity in spheroplast lysates prepared from Saccharomyces cerevisiae was measured by following the incorporation of [14C]mannose from guanosine 5'-diphosphate-[14C]mannose into material precipitable with cold 0.3 M perchloric acid. When enzyme activity was assayed at high concentrations of spheroplast lysate protein (10 mg/ml) in the presence of 7.5 mM MnCl2, a severe inhibition was observed. This inhibition could be relieved by preincubation of the spheroplast lysate at 4 degrees C for 16 to 32 h before assay, by repeated freezing and thawing of the spheroplast lysate, or by the omission of MnCl2 from assay mixtures. The addition of ethylenediaminetetraacetic acid or monovalent cations removed inhibition in the presence of Mn2+. No similar inhibition was observed when a washed membrane fraction was substituted for spheroplast lysate as the source of mannan synthetase. The supernatant fluid obtained by centrifuging spheroplast lysate at 100,000 x g, when added to assay mixtures containing either spheroplast lysate preincubated at 4 degrees C or washed membrane fraction, also caused inhibition of enzyme activity. This inhibition required 7.5 mM MnCl2 and was destroyed by heating the supernatant fluid at 60 degrees C for 10 min, or by trypsin treatment at 30 degrees C. These results indicate the existence of a protein inhibitor of mannan synthesis whose inhibitory activity in spheroplast lysates may be modulated by preincubation at low temperature or by varying the available Mn2+ concentration.

Edetic Acid↗
PubMed1981

Reducing terminus of O-hapten accumulated in a Salmonella montevideo galE mutant.

The O-haptenic polysaccharide of Salmonella montevideo has been reported to contain glyceraldehyde at its reducing terminus. However, O-hapten preparations from a pmi galE mutant contained products of partial hydrolysis of lipopolysaccharide, which in separate experiments gave [3H]glycerol upon treatment with perchloric acid and [3H]aBH4. Further study of the O-hapten reducing terminus suggested that it was actually mannose.

Glycerol↗
PubMed1997

Biochemical basis for glucose-induced inhibition of malolactic fermentation in Leuconostoc oenos.

The sugar-induced inhibition of malolactic fermentation in cell suspensions of Leuconostoc oenos, recently reclassified as Oenococcus oeni (L. M. T. Dicks, F. Dellaglio, and M. D. Collins, Int. J. Syst. Bacteriol. 45:395-397, 1995) was investigated by in vivo and in vitro nuclear magnetic resonance (NMR) spectroscopy and manometric techniques. At 2 mM, glucose inhibited malolactic fermentation by 50%, and at 5 mM or higher it caused a maximum inhibitory effect of ca. 70%. Galactose, trehalose, maltose, and mannose caused inhibitory effects similar to that observed with glucose, but ribose and 2-deoxyglucose did not affect the rate of malolactic activity. The addition of fructose or citrate completely relieved the glucose-induced inhibition. Glucose was not catabolized by permeabilized cells, and inhibition of malolactic fermentation was not observed under these conditions. 31P NMR analysis of perchloric acid extracts of cells obtained during glucose-malate cometabolism showed high intracellular concentrations of glucose-6-phosphate, 6-phosphogluconate, and glycerol-3-phosphate. Glucose-6-phosphate, 6-phosphogluconate, and NAD(P)H inhibited the malolactic activity in permeabilized cells or cell extracts, whereas NADP+ had no inhibitory effect. The purified malolactic enzyme was strongly inhibited by NADH, whereas all the other above-mentioned metabolites exerted no inhibitory effect, showing that NADH was responsible for the inhibition of malolactic activity in vivo. The concentration of NADH required to inhibit the activity of the malolactic enzyme by 50% was ca. 25 microM. The data provide a coherent biochemical basis to understand the glucose-induced inhibition of malolactic fermentation in L. oenos.

Adenosine Triphosphate↗
PubMed1992

A high-mobility-group protein and its cDNAs from Drosophila melanogaster.

We have identified, purified, and characterized a high-mobility-group (HMG) protein and its cDNAs from Drosophila melanogaster. This protein, HMG D, shares most of the characteristics of vertebrate HMG proteins; it is extractable from nuclei with 0.35 M NaCl, is soluble in 5% perchloric acid, is relatively small (molecular weight of 12,000), has both a high basic (24%) and high acidic (24%) amino acid content, and is a DNA-binding protein. HMG D exhibits characteristics of both the vertebrate HMG 1 and 2 class and the HMG 14 and 17 class of proteins. Its amino acid sequence is similar (36% amino acid identity) to that of HMG1, while its size and selective extraction with ethidium bromide are similar to properties of the HMG 14 and 17 class of proteins. HMG D is encoded by a single-copy gene that maps to 57F8-11 on the right arm of chromosome 2. Two transcripts are observed during embryogenesis; the protein is relatively stable throughout development. By the biochemical criteria of size, solubility, and amino acid content, HMG D appears to be the major HMG protein of D. melanogaster.

Amino Acid Sequence↗
PubMed1994

Histone H1 expressed in Saccharomyces cerevisiae binds to chromatin and affects survival, growth, transcription, and plasmid stability but does not change nucleosomal spacing.

Histone H1 is proposed to serve a structural role in nucleosomes and chromatin fibers, to affect the spacing of nucleosomes, and to act as a general repressor of transcription. To test these hypotheses, a gene coding for a sea urchin histone H1 was expressed from the inducible GAL1 promoter in Saccharomyces cerevisiae by use of a YEp vector for high expression levels (strain YCL7) and a centromere vector for low expression levels (strain YCL1). The H1 protein was identified by its inducibility in galactose, its apparent molecular weight, and its solubility in 5% perchloric acid. When YCL7 was shifted from glucose to galactose for more than 40 h to achieve maximal levels of H1, H1 could be copurified in approximately stoichiometric amounts with core histones of Nonidet P-40-washed nuclei and with soluble chromatin fractionated on sucrose gradients. While S. cerevisiae tolerated the expression of low levels of H1 in YCL1 without an obvious phenotype, the expression of high levels of H1 correlated with greatly reduced survival, inhibition of growth, and increased plasmid loss but no obvious change in the nucleosomal repeat length. After an initial induction, RNA levels for GAL1 and H1 were drastically reduced, suggesting that H1 acts by the repression of galactose-induced genes. Similar effects, but to a lower extent, were observed when the C-terminal tail of H1 was expressed.

Animals↗