SEARCH · PubMed Health

Results for “TRICHLOROACETIC ACID”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 703 records · Page 39Linked to original sources

PubMed1994

Determination of adenine nucleotides by fluorescence detection using high-performance liquid chromatography and post-column derivatisation with chloroacetaldehyde.

A novel rapid method for the analysis of adenine nucleotides in cells and tissues using post-column derivatisation with chloroacetaldehyde (CAA) followed by fluorescence detection is described. The CAA is incorporated in the eluent, but only reacts post-column when the temperature is elevated to 100 degrees C. Samples are chromatographed following neutralisation of acid extracts. Examples are given using both trichloroacetic acid extraction for cells in culture, and perchloric acid for murine liver.

Acetaldehyde↗

PubMed1978

Effect of aldosterone on incorporation of amino acids into renal medullary proteins.

Studies on the effects of pretreatment with aldosterone on the incorporation of 3H leucine or 3H methionine into proteins in renal slices were carried out in Joklik-modified minimal essential medium. Administration of aldosterone (2microgram/100 g body wt) to adrenalectomized rats increased 3H leucine incorporation into trichloroacetic acid insoluble fractions of crude homogenates of cortical slices by 15.5 +/- 0.4% and of medullary slices by 53.5 +/- 1.3%. No increase in isotope incorporation was observed in slices of renal papilla or spleen prepared from the same rats. Aldosterone had no effect on the 3H-leucine content of the trichloroacetic acid-soluble fractions of all three renal zones and the spleen. The dose of aldosterone that elicited a half-maximal increase in 3H-methionine incorporation into proteins of renal medullary slices (0.45 microgram of aldosterone/100 g body wt) was indistinguishable from that needed to elicit a halt-maximal increase in the urinary K+/Na+ ratio (0.35 microgram of aldosterone/100 g body wt). Dexamethasone, a potent glucocorticoid, at a dose of 0.8 microgram/100 g body wt did not augment 3H-leucine incorporation into renal medullary proteins but was effective at 8 microgram/100 g body wt. Spirolactone (SC-26304), a potent anti-mineralocorticoid, abolished the effect of aldosterone on amino acid incorporation into medullary proteins when administered at a 100-fold higher dosage [i.e., 80 microgram (per 100 g body wt)]. These results imply that the action of aldosterone on amino acid incorporation is mediated by the mineralocorticoid rather than the glucocorticoid pathway, presumably the mineralocorticoid receptors. Moreover, pretreatment of the rats with actinomycin D (70--80 microgram/100 g body wt) erased the effect of aldosterone (0.8 microgram/100 g body wt) on amino acid incorporation into medullary proteins. In paired experiments with 3H and 35S methionine, aldosterone (0.8 microgram/100 g body wt) increased methionine incorporation into trichloroacetic acid precipitable proteins of subcellular fractions of the renal medulla. The effect of aldosterone on incorporation of methionine into medullary cytosol proteins was analyzed further by polyacrylamide gel electrophoresis at pH 8.3 in tris-glycine buffer. The gel profiles indicate that aldosterone significantly increased methionine incorporation into at least one protein (independent of the isotope) with a molecular weight of approximately 31,000. This increase was inhibited by either pretreatment of the rat with actinomycin D (70--80 microgram/100 g body wt or SC-26304 (80 microgram/100 g body wt). Dexamethasone (0.8 microgram/100 g body wt) did not increase incorporation of methinine into the medullary cytosol proteins resolved by polyacrylamide gel electrophoresis.

Adrenalectomy↗

PubMed1986

Dose-dependent metabolism of trichloroethylene and its relevance to hepatotoxicity in rats.

Fasted male Sprague-Dawley rats pretreated with phenobarbital received an intraperitoneal injection of 0.00, 0.25, 0.50, 0.75, 1.00, 1.50, or 2.00 ml/kg of trichloroethylene (TRI) in corn oil. The metabolic fate of TRI was monitored by measuring its major urinary metabolites 24 hr following the dosing. The hepatotoxic response of TRI was evaluated by determination of the serum transaminase activities (SGOT and SGPT) 24 hr after dosing. Treatment of rats with TRI up to 0.5 ml/kg did not affect the transaminase responses, but significant response was manifested at 0.75 ml/kg dose. Further continuous increases in such responses were induced on exposure to higher doses. Dose-dependent urinary excretions of trichloroethanol and trichloroacetic acid were observed and reached an apparent saturation at 1-1.5 ml/kg dose of TRI. The percentage of dose excreted as trichloroethanol was decreased from 16% at 0.25 ml or 2.8 mmole/kg to 8% at 2 ml or 22.3 mmole/kg dose. The percentage of trichloroacetic acid was decreased from 5 to 2% for the same dose interval. A maximum of only 29% depletion of hepatic glutathione was observed at 2 hr following 1 ml/kg dose of TRI. Similarly, the excretion of urinary mercapturic acid of TRI or thioether was insignificant at any dose level. These results suggest that the conjugation of hepatic glutathione with the electrophilic intermediate of TRI does not seem to be an important determinant for TRI hepatotoxicity nor the major detoxification pathway of its reactive intermediate. TRI produced also a dose-dependent decrease in hepatic microsomal monooxygenase activities as well as cytochrome P-450 content. All these results, when combined, show that there exists an apparent saturable metabolism of TRI involving its activation/deactivation pathways which correspond to an apparent threshold or minimal toxic dose, about 1 ml/kg or 11.15 mmole/kg of TRI for its hepatotoxicity.

Aminopyrine N-Demethylase↗

PubMed1981

Binding of 3'-methyl-N,N-dimethyl-4-aminoazobenzene metabolites to rat liver cytosol proteins and ligandin subunits.

Twenty min after i.p. administration of 3'-[14C]methyl-N,N-dimethyl-4-aminoazobenzene in corn oil to rats, 0.73% of administered radioactivity was present in the liver. Only 0.45% of radioactivity present in liver was recovered in the nuclear fraction, whereas 25% was present in the cytosol fraction. Twenty-seven % of cytosolic radioactivity was trichloroacetic acid precipitable, and 2% was immunoprecipitable with monospecific anti-rat liver ligandin immunoglobulin G. After 3 hr of administration, 3.2% of administered radioactivity was present in the liver, 40% of which was in the cytosol. Although 59% of radioactivity present in liver cytosol was trichloroacetic acid precipitable as compared to 27% at 20 min, the radioactivity precipitated by anti-ligandin immunoglobulin G was still 2%. When liver cytosol obtained from rats after 20 min of 3'-[14C]methyl-N,N-dimethyl-4-aminoazobenzene administration was fractionated on a Sephadex G-75 column, three peaks of radioactivity were observed. When cytosol was subjected to sodium dodecyl sulfate gel electrophoresis and fluorography, radioactivity was mainly associated with 5 proteins with molecular weights of 88,000, 47,000, 41,000, 31,000, and 22,000. When the immunoprecipitate obtained from cytosol with anti-ligandin immunoglobulin G was subjected to sodium dodecyl sulfate gel electrophoresis and fluorography, radioactivity was exclusively associated with the subunit of ligandin with a molecular weight of 22,000. Approximately 90% of the radioactivity in the immunoprecipitate was covalently associated with this subunit. These studies reveal that 3'-methyl-N,N-dimethyl-4-aminoazobenzene or its metabolites are selectively bound to the subunit of ligandin with a molecular weight of 22,000 and four other cytosol proteins in vivo.

Animals↗

PubMed1967

Countercurrent-distribution studies on histones.

1. The possibilities of fractionating histones and histone fractions by means of countercurrent distribution between two phases formed by water and butan-2-ol, in the presence of various concentrations of trichloroacetic acid, have been examined. 2. Although the principal histone fractions differ considerably in their partition ratios, a satisfactory resolution of the principal histone fractions from the whole histone has not been achieved. 3. The histone fractions obtained by other methods can be resolved with suitable concentrations of trichloroacetic acid. Besides the main peak several subsidiary peaks are obtained in most cases, the composition of which corresponds with others of the main fractions. 4. The method is therefore capable of removing from the principal fractions as previously prepared contamination by other fractions. 5. Except in one case, no fraction with composition unlike other fractions has been obtained. In several cases the material isolated from the principal peak behaves as a single component on running again. In two cases fractions with similar compositions were distinguished by countercurrent distribution.

Acids↗

PubMed1966

Electron microscopy of Staphylococcus aureus cell wall lysis.

Virgilio, Rafael (Escuela de Química y Farmacia, Universidad de Chile, Santiago, Chile), C. González, Nubia Muñoz, and Silvia Mendoza. Electron microscopy of Staphylococcus aureus cell wall lysis. J. Bacteriol. 91:2018-2024. 1966.-A crude suspension of Staphylococcus aureus cell walls (strain Cowan III) in buffer solution was shown by electron microscopy to lyse slightly after 16 hr, probably owing to the action of autolysin. The lysis was considerably faster and more intense after the addition of lysozyme. A remarkable reduction in thickness and rigidity of the cell walls, together with the appearance of many irregular protrusions in their outlines, was observed after 2 hr; after 16 hr, there remained only a few recognizable cell wall fragments but many residual particulate remnants. When autolysin was previously inactivated by trypsin, there was a complete inhibition of the lytic action of lysozyme; on the other hand, when autolysin was inactivated by heat and lysozyme was added, a distinct decrease in the thickness of the cell walls was observed, but there was no destruction of the walls. The lytic action of lysozyme, after treatment with hot 5% trichloroacetic acid, gave rise to a marked dissolution of the structure of the cell walls, which became lost against the background, without, however, showing ostensible alteration of wall outlines. From a morphological point of view, the lytic action of autolysin plus lysozyme was quite different from that of trichloroacetic acid plus lysozyme, as shown by electron micrographs, but in both cases it was very intense. This would suggest different mechanisms of action for these agents.

Bacteriolysis↗

PubMed1984

Protein dependence of digoxin determination on the Abbott-TDX.

The protein dependence of digoxin quantitation on the Abbott TDX was evaluated. An inverse relationship was found to exist between protein concentration and digoxin levels in samples that were deproteinized with 50 g/L trichloroacetic acid prior to assay. This was especially evident in the protein range from 30-60 g/L where a 30% decrease in digoxin concentration was observed. Recovery studies using 125I-digoxin showed that this decrease could be totally accounted for by a decreased recovery of digoxin in the trichloroacetic acid supernatant. The serum-based calibrators used to establish the standard curve on the instrument showed similar recoveries to serum samples. The reduced recovery does not pose accuracy problems as long as the protein concentrations of the patient samples and calibrators are similar. The clinical and operational implications of this observation are discussed.

Blood Proteins↗

PubMed1965

THE INCORPORATION OF GLYCEROL AND LYSINE INTO THE LIPID FRACTION OF STAPHYLOCOCCUS AUREUS.

1. Incubation of washed cells of Staphylococcus aureus with [1-(14)C]glycerol results in the incorporation of glycerol into the lipid fraction of the cells. The rate of incorporation is increased by the presence of glucose and amino acids. The presence of amino acids increases incorporation into the fraction containing O-amino acid esters of phosphatidylglycerol. 2. Glycerol, incorporated into washed cells by incubation with glycerol, glucose and amino acids, is rapidly released from the lipid fraction when cells are incubated at low suspension densities in buffer. 3. Of nine amino acids tested, only lysine is significantly incorporated into the lipid fraction. The incorporation is increased by the presence of glycerol, glucose and other amino acids, especially aspartate and glutamate. 4. The incorporation of lysine is increased by the addition of puromycin at concentrations that inhibit protein synthesis. Chloramphenicol does not increase the incorporation of lysine but abolishes the enhancing effect of puromycin. 5. The enhancing effect of puromycin is accompanied by a similar increase in the incorporation of lysine into the fraction soluble in hot trichloroacetic acid. 6. Lysine is incorporated into the lipid fraction that contains O-amino acid esters of phosphatidylglycerol and corresponds in properties to phosphatidylglyceryl-lysine. 7. Lysine is rapidly released from the lipid of cells incubated in buffer only at low suspension densities. 8. Incubation of cells with the phosphatidylglyceryl-lysine fraction does not lead to the appearance of free lysine or to incorporation into the fraction insoluble in hot trichloroacetic acid.

Amino Acids↗

PubMed1975

Biosynthesis of starch. Formation of a glucoproteic acceptor by a potato non-sedimentable preparation.

1. A non-sedimentable fraction of potato tuber has been found to catalyze [14C]glucose transfer from [14C]glucose 1-phosphate to an endogenous proteic acceptor in the absence of added primer. This transfer is activated by Mn2+. 2. The labeled glucosylated product formed is trichloroacetic acid insoluble and sensitive to proteolytic and amylolytic digestions. It appears to be a glucoprotein with glucosyl chains bound to the peptide portion of the molecule through an unknown linkage. 3. The carbohydrate portion of the glucoprotein can be released by prolonged incubations with the enzymatic preparation, and becomes in turn, trichloroacetic acid soluble and alcohol precipitable. 4. Both products, the glucoprotein as well as the alpha-1,4-glucan that seems to arise from the enzymatic cleavage of the former, can be used as primers by the transglucosylating system with ADP[14C]glucose, UDP[14C]glucose or GDP[14C]glucose as glucosyl donors. The results presented in this paper are the first demonstration of soluble glucosyl transferases with the same glucose donor specificity to that of the particulate starch synthetase. 5. This report presents further evidence in favor of the assumption of a glucoproteic intermediate in alpha-a,4-glucan synthesis initiation.

Adenosine Diphosphate Glucose↗

PubMed1985

Purification of thyroid lysosomes by colloidal silica density gradient centrifugation.

A procedure was devised for fractionating crude thyroid lysosomal particles (P750-15,000) by self-forming density gradient centrifugation with colloidal silica. Two discrete particle-containing peaks were observed, based on 131I-labeling and acid phosphatase activity: a heavy peak (density, 1.11-1.12) and a light peak (density, 1.05). Ultrastructural analysis revealed that the heavy peak consisted almost entirely of lysosomes, whereas the light peak represented a heterogeneous mixture of small vesicles and fragments of other intracellular organelles. In thyroids removed from rats 30 min after 131I injection, almost all of the 131I was present in the low density peak. This 131I appeared on sucrose density gradient centrifugation as a 19S peak, and it was almost completely insoluble in trichloroacetic acid. This was interpreted as indicating that the low density peak contained pinocytotic vesicles. In thyroids removed 4 days after 131I injection, the radioactivity appeared largely in the high density peak. Both the trichloroacetic acid solubility and the pattern on sucrose density gradient centrifugation indicated that the [131I] thyroglobulin had undergone extensive proteolysis. Thyroglobulin proteolytic activity was found primarily in the high density particles and to only a small extent in the low density particles. Studies performed at intervals after 131I injection combined with double labeling (131I and 125I) experiments provided evidence that radioactivity was transferred from the low density to the high density particles. Heterogeneity existed within the dense peak, related to the degree of thyroglobulin degradation, as it was observed that thyroid lysosomes become denser with increasing proteolysis of thyroglobulin. The acid phosphatase in the low density particles could be distinguished from that in the high density (lysosomal) particles by its elution pattern on Sephadex G-200 column chromatography, its response to freezing and thawing, and its reactivity with p-nitrophenylphosphate. It was concluded, therefore, that the acid phosphatase in the low density fraction was derived from prolysosomal structures such as vesiculated Golgi-endoplasmic reticulum-lysosomes. The prolysosomal acid phosphatase associated with the low density fraction appeared to be a large membrane-bound molecule which could be transformed into lysosomal acid phosphatase by incubation at pH 5.0.

Acid Phosphatase↗

PubMed1975

Physical-chemical properties of precipitated and fractionated allergens from Mycobacterium bovis.

Seven allergens were prepared from cultures of Mycobacterium bovis. The culture filtrates were divided in half and each aliquot precipitated with either ammonium sulfate or trichloroacetic acid to prepare purified protein derivatives (PPD). These samples of PPD-bovis were analyzed for nitrogen, carbohydrate, RNA and DNA. Physical tests, such as: cellulose acetate electrophoresis, disc gel electrophoresis, ultracentrifugation, isoelectricfocusing and gel filtration were also performed. Precipitation with ammonium sulfate provided PPD's with less impurities than those precipitated with trichloroacetic acid although there was little difference in the allergenic activity of the products precipitated by either method. Several lots of PPD-bovis were fractionated by means of ultrafiltration and the fractions analyzed by many of the above chemical and physical tests as well as tests for amino acid composition and allergenic activity. The greatest amount of protein was found in the fractions with an apparent molecular weight in excess of 300,000. The carbohydrate was usually distributed in proportion to the amount of protein in each fraction while the nucleic acids were predominately found in the higher molecular weight fractions. The amino acid analysis and allergenic activity of the various molecular weight fractions provided data that would support the theory that the various fractions are polymers of a small molecular weight sub-unit. The number of amino acid residues were calculated and the minimum molecular weight of the tubercular protein estimated to be 8700. The estimated molecular weights of the fractions and the amino acid data concur with those previously reported for proteins from other mycobacteria.

Allergens↗

PubMed2005

Human papillomavirus: burden of illness and treatment cost considerations.

The monetary and personal costs to society of human papillomavirus (HPV) infection are enormous. In order to make a comparison of different treatment methods we reviewed the entire literature on HPV treatment from January 1966 to December 2003 using MEDLINE, with particular reference to published meta-analyses, randomized controlled and comparative studies. Patient-applied therapies offer patients the possibility of convenient and, on the whole, pain-free treatment. Podofilox (podophyllotoxin) and salicylic acid for genital and extragenital warts, respectively, have the additional advantage of being the most cost-effective treatments and, on this basis, they are to be commended as appropriate first-line agents. The second-line treatment of choice for common warts is cryotherapy. For recalcitrant common warts possible options include inosine pranobex with cryotherapy or electrosurgery, imiquimod with paring and occlusion, intralesional bleomycin, or diphencyprone. Alternative first-line and second-line treatments for genital warts would be either some form of surgical removal or imiquimod. The first option may be the cheapest but this has to be balanced against a degree of post-operative morbidity. Limited data from comparative studies do not show any clear difference in efficacy between cryotherapy, trichloroacetic acid, scissor excision, electrosurgery, and laser surgery in the treatment of genital warts, and the cost effectiveness of these therapies is probably similar to that of imiquimod. Cryotherapy and trichloroacetic acid are relatively expensive and inconvenient for patients and should be reserved as third-line treatments with certain exceptions, such as cryotherapy for meatal warts. The duration of treatment is significantly related to the number of warts present, the area covered by the warts, and the length of time the warts have been present. For recalcitrant anogenital warts third-line treatment options that show promise include surgery in combination with imiquimod or cidofovir cream. For squamous intraepithelial lesions that cannot easily be excised or physically ablated current treatment options include imiquimod and fluorouracil cream. The latter is an inexpensive option but causes the greatest morbidity. It is hoped that cidofovir may be added to this list if it becomes commercially available, and that protective and therapeutic HPV vaccines will transform the management of HPV in the future.

AIDS-Related Opportunistic Infections↗

PubMedDate not supplied

Bioactivation of tetrachloroethylene. Role of glutathione S-transferase-catalyzed conjugation versus cytochrome P-450-dependent phospholipid alkylation.

The metabolism of [14C]tetrachloroethylene (Tetra) and its metabolite S-(1,2,2-trichlorovinyl)-L-cysteine (TCVC) was investigated with in vitro systems to substantiate metabolic pathways of Tetra deduced from in vivo experiments. In the presence of NADPH, rat hepatic microsomal fractions metabolized Tetra to soluble metabolites, which were identified as trichloroacetic acid and oxalic acid by gas chromatography/mass spectroscopy and a metabolite largely bound to microsomal macromolecules. The majority of the alkylated macromolecules were identified as N-trichloroacetylated phospholipids by high performance liquid chromatography and GC/MS. When Tetra was incubated with hepatic microsomes and cytosol in the presence of 10 mM glutathione, but in the absence of NADPH, the formation of a polar metabolite other than trichloroacetic acid and oxalic acid was observed. This metabolite was identified, after hydrolysis to the corresponding cysteine conjugate, as S-(1,2,2-trichlorovinyl)-glutathione (TCVG). Microsomal GSH S-transferases catalyzed TCVG formation more efficiently than cytosolic GSH S-transferases; the competitive substrate 1-chloro-2,4-dinitrobenzene inhibited TCVG formation. In the presence of both NADPH and GSH, TCVG formation in microsomes was decreased, indicating that oxidative metabolism and GSH conjugation of Tetra are competitive reactions. The Tetra metabolite TCVC was cleaved by bacterial cysteine conjugate b-lyase to dichloroacetic acid and pyruvate. The obtained results substantiate the postulated pathways of Tetra biotransformation and demonstrate that both oxidative and conjugative reactions occur in hepatic Tetra metabolism. Phospholipid alkylation, which occurs during oxidative metabolism, may be a deactivation reaction, whereas TCVG formation, renal metabolism to TCVC, and cleavage of TCVC by b-lyase under formation of mutagenic intermediates may contribute to the nephrocarcinogenic effect of Tetra.

Alkylation↗

PubMed1996

Stability of invertase in reverse micelles.

The stability of invertase was studied under various conditions, including at 75 degrees C, in presence of stabilizers (sorbitol and glycerol) at 75 degrees C, and in the presence of denaturants (urea and trichloroacetic acid) at 37 degrees C in reverse micelles. Stability of the invertase in reverse micelles was found to be improved over that of the enzyme in bulk aqueous solution. Sorbitol could enhance enzyme stability as it does in the bulk aqueous system. The stabilizing effect of glycerol was reduced in reverse micelles. The denaturation pattern of urea remains unaltered. However, the denaturation effect of trichloroacetic acid has been reduced in reverse micelles.

Enzyme Stability↗

PubMedDate not supplied

Epinephrine-induced cardiac arrhythmias in rabbits exposed to trichloroethylene: potentiation by caffeine.

Approximately 200 000 industrial workers are exposed to trichloroethylene in the United States. Individuals intoxicated with trichloroethylene are known to develop cardiac arrhythmias. Caffeine is known to be a cardiac stimulant and is one of the drugs most widely used by the American population. Therefore, it was of interest to study the effect of caffeine on the arrhythmogenicity of trichloroethylene. Rabbits were treated with a vehicle control (1 mL/kg, ip) or caffeine (10 mg/kg, ip, 30 minutes prior to exposure) and exposed for one hour to 6000 ppm trichlorethylene under dynamic airflow conditions. Epinephrine was infused until arrhythmias occurred after 7.5, 15, 30, 45 and 60 minutes of exposure and also 15 and 30 minutes post-exposure. Serial blood samples were collected at these time points and analyzed for trichloroethylene and the two major metabolites, trichloroethanol and trichloroacetic acid. Rabbits treated with caffeine and exposed to trichloroethylene developed more arrhythmias in response to epinephrine than rabbits exposed to trichloroethylene alone, and the arrhythmias occurred sooner and in response to lower doses of epinephrine. Caffeine treatment had no effect on trichloroethylene blood concentration, but significantly decreased trichloroethanol blood levels after 45 and 60 minutes of exposure to trichloroethylene. Caffeine also reduced blood levels of trichloroacetic acid. The data indicate that caffeine can potentiate the arrhythmogenicity of trichloroethylene in rabbits.

Animals↗

PubMed1986

Trapping and partial characterization of an adduct postulated to be the covalent catalytic ternary complex of thymidylate synthase.

The proposed mechanism of action of thymidylate synthase envisages the formation of a covalent ternary complex of the enzyme with the substrate dUMP and the cofactor 5,10-methylenetetrahydrofolate (CH2H4folate). The proposed structure of this adduct has been based by analogy on that of the covalent inhibitory ternary complex thymidylate synthase-FdUMP-CH2H4folate. Our recent success in using the protein precipitant trichloroacetic acid to trap the latter complex and covalent binary complexes of the enzyme with FdUMP, dUMP, and dTMP led to the use of this technique in attempts to trap the transient putative covalent catalytic ternary complex. Experiments performed with [2-14C]dUMP and [3',5',7,9-3H]CH2H4folate show that both the substrate and the cofactor remained bound to the protein after precipitation with trichloroacetic acid. The trapped putative covalent catalytic complex was subjected to CNBr fragmentation, and the resulting peptides were fractionated by reverse-phase high-pressure liquid chromatography. The isolated active site peptide was shown to retain the two ligands and was further characterized by a limited sequence analysis using the dansyl Edman procedure. The inhibitory ternary complex, which was formed with [14C]FdUMP and [3H]CH2H4folate, served as a control. The active site peptide isolated from the CNBr-treated inhibitory ternary complex was also subjected to sequence analysis. The two peptides exhibited identical sequences for the first four residues from the N-terminus, Ala-Leu-Pro-Pro, and the fifth amino acid residue was found to be associated with the labeled nucleotides and the cofactor.(ABSTRACT TRUNCATED AT 250 WORDS)

Carbon Radioisotopes↗

PubMed1980

The reverse single radial immunodiffusion technique for detecting antibodies to Dermatophilus congolensis.

The reverse single radial immunodiffusion technique was used to detect Dermatophilus congolensis antibody in sera collected from animals previously infected to varying levels with D congolensis. Ammonium sulphate and trichloroacetic acid extracts of five different strains of D congolensis obtained from different geographical locations were used as antigens. All the extracts showed variations in their sensitivities in detecting D congolensis antibody in the various serum samples. Multiple antibodies were detected by some extracts while some showed negative antibody reaction to all extracts. Two extracts also showed cross-reactions with the serum from an animal that was infected by Nocardia species. Trichloroacetic acid extracts of all the strains were found to be more active serologically, detecting antibody in more sera and giving sharper and clearer reactions than ammonium sulphate extracts.

Actinomycetales↗

PubMed1976

Incorporation of inorganic sulfate in rat-liver Golgi.

Partial subcellular distribution and specifically the incorporation of 35SO4 in the Golgi apparatus of rat liver was studied. The isolated Golgi fraction was placed on a further sucrose gradient for subfraction and in all samples the total incorporated label, the trichloroacetic-acid-soluble and insoluble, and chloroform/methanol-soluble and insoluble amounts of label were measured. Approximately 2.3% of the total injected 35S was found in the liver, of which 2% was localized in the isolated Golgi fraction. Further subfractionation of the Golgi has shown that the majority of the 35S is localized at densities 1.12-1.13 g/cm3 in the gradient. In the isolated Golgi fraction 85% of the label was present in the trichloroacetic-acid-soluble and 15% in the insoluble part. Approximately 1% of the label in the Golgi fraction was soluble in chloroform/methanol. On the bases of radioactivity per weight of protein and total radioactivity, the Golgi fractions had the highest activity, except the first supernatant which had higher radioactivity. Briefly, a significant amount of the 35SO4 can be found in the isolated rat liver Golgi 15 min after the injection of the label, and the majority of this label is localized in the material sedimenting at density 1.12-1.13 g/cm3 after subfractionation of the Golgi apparatus.

Animals↗