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PubMed1980

Adenosine diphosphate ribosylation of histone H1 by purified calf thymus polyadenosine diphosphate ribose polymerase.

The mechanism of poly ADPR synthesis and the transfer of poly ADPR to histone H1 molecule by electrophoretically homogenous calf thymus poly ADPR polymerase containing DNA was examined. 1) An acid insoluble radioactive complex (I) was obtained after incubation of purified enzyme with [3H] NAD. The stability of (I) was examined by SDS-polyacrylamide gel electrophoresis. The complex (I) was stable against acid, SDS, urea, DNase and RNase, but labile against pronase, trypsin, alkali and snake venom phosphodiesterase treatment. The molecular weight of (I) was about 130 000 daltons estimated by SDS-gel electrophoresis. The radioactive products of successive alkali, venom phosphodiesterase and Pronase hydrolysis of (I) were PR-AMP and AMP. The mean chain length of poly ADPR of (I) was 20--30. These results suggest that the complex (I) is poly ADP-ribosylated poly ADPR polymerase. 2) Besides (I), a second radioactive peak (II) was observed when acid insoluble products obtained from an incubation mixture containing purified poly ADPR polymerase, [3H] NAD and purified histone H1 were analyzed on SDS-polyacrylamide gel electrophoresis. The molecular weight of (II) was estimated to be about 23 000 daltons. The complex (II) is eluted like histone H1 on CM-cellulose columns and hydrolyzed by alkali, trypsin and snake venom phosphodiesterase but not by DNase, or RNase. The comples (II) was extracted selectively by 5 per cent perchloric acid or 5 per cent trichloroacetic acid from mixture of (I) and (II). The mean chain length of poly ADPR of complex (II) and 5--20; these results suggest that the complex (II) is poly ADP-ribosylated histone H1. 3) Results 1) and 2) indicate that purified DNA containing, thus DNA independent, poly ADPR polymerase catalyzes two different reactions, the ADPR transfer onto the enzyme itself and onto histone H1 and the elongation of ADPR chains. Dimeric forms of ADP-ribosylated histone H1 was not observed. Free poly ADPR was observed only when very small quantities of enzyme were used for incubation.

Animals↗

PubMed1998

Isoaspartate in chrondroitin sulfate proteoglycans of mammalian brain.

Mammalian brain contains a high mass protein (HMAP) that is unusually rich in atypical L-isoaspartyl (isoAsp) linkages. HMAP has now been purified from bovine brain by anion exchange, hydroxylapatite, and size exclusion chromatography. It is self-aggregating, acidic, and soluble in 5% trichloroacetic acid. Treatment with chondroitinase ABC eliminates the self-aggregation of HMAP and generates several distinct core proteins with estimated masses of 350-450 (doublet), 180, and 100 kDa, indicating that it is composed mainly of chondroitin sulfate proteoglycans (CSPGs). Most of the isoAsp resides in the 350-450-kDa core protein, which was identified by immunoblotting as phosphacan, a CSPG abundant in adult brain. The regional distribution and developmental profile of HMAP in rat brain support this identification. The 180-kDa core protein contains a tenascin-R-related molecule, consistent with recent observations that phosphacan forms a tight complex with tenascin-R. The average phosphacan molecule in adult brain contains at least seven isoAsp sites. Molecular heterogeneity due to isoAsp may explain some of the complex binding properties phosphacan exhibits with its natural ligands. Formation of isoAsp may be important in the roles that phosphacan and other CSPGs play in development of the nervous system.

Animals↗

PubMed1973

Comparative transport activity of intact cells, membrane vesicles, and mesosomes of Bacillus licheniformis.

Sodium ion was shown to stimulate strongly the transport of l-glutamic acid into cells of Bacillus licheniformis 6346 His(-). Lithium ion had a slight capacity to replace Na(+) in this capacity, but K(+) was without effect. Three of five amino acids tested. l-glutamic acid, l-aspartic acid, and l-alanine, were concentrated against a gradient in the cells. Intracellular pools of these amino acids were extractable with 5% trichloroacetic acid. Pools of l-histidine and l-lysine could not be detected. No evidence of active transport of lysine into cells could be detected, and histidine was taken up in the absence of chloramphenicol but not in its presence. The uptake of glutamic acid by membrane vesicle preparations was strongly stimulated by reduced nicotinamide adenine dinucleotide (NADH) and to a lesser extent by succinate. The presence of phenazine methosulfate increased uptake in the presence of succinate. Either l- or d-lactate and adenosine triphosphate were without effect. None of these compounds stimulated the uptake of glutamic acid by mesosomes, although some mesosome preparations contained separable membrane which was very active. NADH strongly stimulated the uptake of aspartic acid and alanine by membrane vesicles but had only a slight effect on the uptake of histidine and lysine. No evidence of active transport of any of the amino acids into mesosomes could be detected either in the presence or absence of NADH. NADH stimulation of the uptake of glutamic acid by membrane vesicles was destroyed by exposure to light of 360 nm; this inactivation was reversible by vitamin K(2(5)) or K(2(10)). Sodium ion stimulated transport of glutamic acid by membrane vesicles.

Alanine↗

PubMed1967

Physiology of rickettsiae. VII. Amino acid incorporation by Coxiella burnetii and by infected hosts.

Protein synthesis, in terms of (14)C-labeled amino acid incorporation into a hot trichloroacetic acid fraction, was studied in cell-free preparations of Coxiella burnetii, and in uninfected and Q fever-infected guinea pig and chick embryo hosts. Purified and disrupted suspensions of C. burnetii incorporated (14)C-labeled l-leucine, l-phenylalanine and algal hydrolysate. Livers of infected guinea pigs and chick embryos had a greater incorporation rate at the height of infection than comparable preparations from uninfected animals. As chick embryonic development continued during infection, the rate of incorporation progressively decreased below that of uninfected embryos.

Amino Acids↗

PubMedDate not supplied

Action of aldosterone on cultured renal collecting duct cells during the latent period.

The effects of aldosterone on protein synthesis in the latent period were investigated on cultured renal collecting duct cells from neonatal rabbit kidneys. Tissue was incubated with radioactively labelled uridine and amino acids and then precipitated with trichloroacetic acid in order to determine the intracellular precursor pool and identify new synthesis of RNA and protein. During the latent period, aldosterone increased the intracellular radioactive uridine pool and total radioactive RNA content already 20 and 60 min after its application; conversely 40 min after aldosterone introduction, no stimulation was found. Further experiments revealed that the intracellular radioactive amino acid pool was generally increased by aldosterone after 20, 40 and 60 min, while a distinct increased radioactive protein content was found to be induced by aldosterone only after 40 min. This indicates that aldosterone increases the uptake of RNA and protein precursors and the new synthesis of RNA and proteins. These events seem to to be regulated not continuously but intermittently. The induced proteins possibly take part in the mediation of the early hormone response. Experiments with the aldosterone antagonist, spironolactone, provide evidence for the specificity of the described hormone effects. The results after application of the Na+ channel blocker, amiloride, and the Na+/K(+)-ATPase inhibitor, G-strophanthin, indicate that the aldosterone effects are controlled by Na+ channels and Na+ pumps and therefore by the intracellular Na+ content. The inhibitory effect of cycloheximide on the aldosterone-induced protein synthesis indicates the role of these proteins on the hormone-stimulated Na+ transport.

Aldosterone↗

PubMed1985

The influence of temperature on the functions of cultured Sertoli cells.

Three functions of Sertoli cells were examined with cells from rats aged 13 and 25 days at 34 C, 38 C, and 40 C, namely protein synthesis (incorporation of amino acids into material precipitated by trichloroacetic acid), transport of alpha-aminoisobutyric acid, and production of lactate. A fourth function, namely production of cAMP was examined at two temperatures (34 C and 38 C) in cells from rats aged 25 days. In all cases, activity was greater at 38 C than at 34 C and greater at 40 C than at 38 C. Lysate of Sertoli cells showed similar differences in protein synthesis at the three temperatures, again at both ages. Protein synthesis was higher at 38 C than at 34 C in Sertoli cell-enriched tubules from rats aged 25 days and in Sertoli cells from normal rats of the same age cultured on rat tail collagen. The difference in protein synthesis at the two temperatures was seen whether the cells were cultured, before the experiment, for 7 days at 38 C or at 34 C. Production of cAMP by Sertoli cells was greater at 38 C than at 34 C. It is concluded that Sertoli cells do not show in vitro any inhibitory effect of body temperature on any of the functions tested, but on the contrary, are more active at body than at scrotal temperature. The possible significance of the differences seen is discussed.

Aminoisobutyric Acids↗

PubMed1982

Reaction products of aquatic humic substances with chlorine.

A major concern of the chlorination of aquatic humic materials is the ubiquitous production of trihalomethanes. A large number of other chlorinated organic compounds, however, have been shown to be formed by chlorine's reaction with humic substances. In this study, humic material was concentrated from a coastal North Carolina lake and chlorinated at a chlorine to carbon mole ratio of 1.5 at pH 12. A high pH was necessary for complete dissolution of the humic material and for production of adequate quantities of oxidation and chlorination products for extraction, separation and mass spectrometric identification. After concentration in ether, samples were methylated, separated with a 50-m OV-17 glass capillary column or a 25 m SP-2100 fused-silica column and identified. A Hewlett-Packard 5710A gas chromatograph interfaced to a VG Micromass 7070F double-focusing mass spectrometer was used. Low resolution, accurate mass measurements were made with a combined EI-Cl source. The ability to do low resolution, accurate mass measurements made possible a rapid scan function necessary for capillary column gas chromatography. Accurate mass measurements allowed increased confidence in the identification of compounds, most of which are not available as standards. The products identified in these studies were chlorinated aliphatic straight-chain acids dominated by di- and trichloroacetic acid and the chlorinated dicarboxylic acids: succinic, fumaric and maleic acids. Chlorinated and unchlorinated aliphatic mono- and dicarboxylic acids and unchlorinated polycarboxylic aromatic acids comprise the remaining bulk of the compounds identified.

Chemical Phenomena↗

PubMed1990

Effect of amiodarone on non-deiodinative pathway of thyroid hormone metabolism.

Amiodarone, an iodine containing anti-arrhythmic drug, causes a significant decrease in molar ratio of daily production rates of T3 and T4 from 0.75 in controls to 0.36 in amiodarone-treated rabbits. A model was constructed from the above data which showed that metabolism of T4 via non-deiodinative pathways (e.g. tetraiodothyroacetic acid and/or conjugates) increased from 29% in untreated controls to 66% in amiodarone-treated rabbits. In this study, we have examined the metabolic clearance rate of tetraiodothyroacetic acid in rabbits given amiodarone (20 mg.kg-1.day-1 ip for 3 weeks) or saline (controls). Serum amiodarone and desethylamiodarone levels under the above experimental conditions were 0.20 +/- 0.067 and 0.17 +/- 0.058 mg/l, respectively, which were in the near-therapeutic range observed in humans. Control and amiodarone-treated rabbits were administered [125I]-tetraiodothyroacetic acid (10 muCi/rabbit) iv and blood was collected at 0.5, 1, 2, 4, 6, 10, 32 and 48 h. Serum tetraiodothyroacetic acid radioactivity was determined by trichloroacetic acid precipitation and ethanol extraction and metabolic clearance rates were calculated from the area under the curve of computer fits to tetraiodothyroacetic acid radioactivity data. Amiodarone treatment decreased metabolic clearance rates significantly from 0.107 +/- 0.008 in controls to 0.074 +/- 0.009 l/day in amiodarone-treated rabbits (p less than 0.05). However, when expressed per unit body weight (1.day-1.kg-1), the metabolic clearance rates were not significantly different between the controls and amiodarone-treated rabbits. The terminal serum elimination half-life in the two groups were similar (32.0 +/- 6.7 h in controls vs 49.2 +/- 12.4 h in amiodarone-treated).(ABSTRACT TRUNCATED AT 250 WORDS)

Amiodarone↗

PubMed1998

Metabolic interaction between toluene, trichloroethylene and n-hexane in humans.

OBJECTIVES: This human experimental study describes the mutual metabolic interaction between toluene, trichloroethylene, and n-hexane. METHODS: Eight healthy male volunteers were exposed to combinations of toluene (1.5 or 4 mg/min), trichloroethylene (1.5 or 4 mg/min), and n-hexane (0.3 or 1.0 mg/min) for 60 min. End exhaled air concentrations were measured before and up to 240 min after the start of exposure. The urinary excretion of hippuric acid, o-cresol, trichloroethanol, trichloroacetic acid, and 2,5-hexanedione was measured before and up to 270 min after the start of the exposures. RESULTS: When the low dose rates were combined, the end exhaled concentrations were at or below the detection limit, while an increase in the dose rate of toluene increased the area under the end exhaled air concentration curve (AUC) of toluene, trichloroethylene, and n-hexane by factors of 44 (16-117) [geometric mean and 95% confidence interval], 12.8 (4.1-40.0), and 2.2 (1.2-4.1), respectively. Trichloroethylene, in turn, increased the AUC 5.0 (1.9-13.4), 25.8 (8.2-80.8) and 2.9 (1.6-5.4), respectively, whereas the corresponding values for n-hexane were 1.9 (0.7-5.1), 1.5 (0.5-4.6), and 3.2 (1.8-5.9). An 18 (range 2-34)% decrease in hippuric acid was the only interaction measured in the metabolite excretion. No correlation occurred between the individual measures of the end exhaled concentrations or the excretion of metabolites. CONCLUSIONS: The study shows that the threshold for the flow-limited metabolism of the 3 solvents in humans is exceeded at liver dose rates corresponding to inhalation exposure at occupational exposure limits. At these levels there are metabolic interactions between the 3 solvents.

Adult↗

PubMed1988

Role of ATP in mitochondrial protein import. Conformational alteration of a precursor protein can substitute for ATP requirement.

The role of nucleoside triphosphates (NTPs) in the import of porin into the mitochondrial outer membrane was investigated with two forms of the porin precursor: the in vitro synthesized biosynthetic precursor (bs-porin) and a water-soluble form of porin (ws-porin) obtained by subjecting the membrane-derived porin to an acid-base treatment (exposure to trichloroacetic acid, followed by alkali and rapid neutralization). The import of ws-porin into mitochondria did not require NTPs, whereas the import of bs-porin required NTPs. In other characteristics, such as binding to a specific receptor protein on the mitochondrial surface, two-step insertion into the outer membrane, and formation of specific membrane channels, ws-porin was indistinguishable from bs-porin. Thus, the acid-base treatment applied in the preparation of ws-porin can substitute for the NTP-requiring step in mitochondrial protein import. We conclude that NTPs are required for unfolding mitochondrial precursor proteins ("translocation competent folding").

Adenosine Triphosphate↗

PubMed1977

Effects of maleic acid administration on urinary excretion of DCEC, and on tissue protein, in the rat.

Administration of maleic acid to rats caused increased urinary excretion of S-(1,2-dicarboxyethyl)cysteine [DCEC] and increased binding of maleic acid to tissue proteins. The trichloroacetic acid precipitate from a combined fraction of supernatant and microsome gave the maximum amount of DCEC after hydrolysis. It would appear that aminoaciduria produced by maleate was partially due to increased destruction of some succinylated tissue proteins.

Amino Acids, Dicarboxylic↗

PubMed1980

Enzyme-linked immunosorbent assay for group B streptococcal antibodies.

We report here on the development of enzyme-linked immunosorbent assays (ELISAs) for antibodies to types II and III group B streptococci. Streptococcal antigens were prepared by trichloroacetic acid extraction and fractional alcohol precipitation. Microtiter wells were coated with antigen in 0.1 M carbonate buffer at pH 9.6. Lyophilization was found to be an essential step for efficient binding of the streptococcal antigens. After incubation with antibody-containing rabbit serum, bound antibody was detected with peroxidase-labeled goat anti-rabbit immunoglobulin G. Optimal antigen concentrations were 200 micrograms/ml for type II and 100 micrograms/ml for type III. An ELISA is also described that uses intact bacteria as antigen. Hyperimmune rabbit serum reacted at a titer in excess of 512 against trichloroacetic acid-soluble antigen and 4,096 against whole bacteria. Sera from human subjects were also tested. Most human sera contained antibody which bound to intact bacteria but not to trichloroacetic acid-solubilized streptococcal antigens. Antibody titers in human sera against intact bacteria correlated very well with opsonic antibody activity measured in a chemiluminescence assay.

Animals↗

PubMed1996

Comparison of the effect of various chemical peeling agents in a mini-pig model.

BACKGROUND: With the advent of newer chemical peels, there is now a wide range of peeling agents that can be applied on specific patients. OBJECTIVE: The purpose of this study was to closely examine the more common chemical peeling agents at different concentrations. METHODS: The study methods were carried out by thoroughly cleansing the skin surface with acetone. Different concentrations of the chemical peels were applied on different skin areas (2 x 2 cm each) and left on the skin for 15 minutes: phenol-Bakers, 25%, 50%, 75%, 88%; trichloroacetic acid, 25%, 50%, 75%; glycolic acid, 50%, 70%; and pyruvic acid, 50%, 100%. Serial biopsies were taken from each peeling site at 1, 7, and 21 days post-peel. Biopsies were then evaluated for epidermal changes, inflammation, and collagen deposition. RESULTS: The results show that Bakers phenol peel caused the most inflammation and nonspecific reaction, and in addition, a proportionate amount of new collagen deposition. Plus, increasing concentrations of phenol and TCA caused increasing amount of epidermal sloughing and inflammation after 1 day post-peel. The extent of reaction from the phenol and TCA was directly proportional to the collagen deposition at 21 days. CONCLUSIONS: The glycolic acid and pyruvic acid caused minimal nonspecific reaction. However, the collagen deposition caused by the glycolic acid and pyruvic acid was disproportionately increased suggesting a direct stimulatory effect by the two agents.

Animals↗

PubMed2002

Measurement of low level membrane proteins using bicinchoninic acid: modified procedures to eliminate interfering substances.

Accurate determination of low levels of protein in samples containing large amounts of interfering substances is rather difficult. Precipitation-bicinchoninic acid (BCA) assay as reported can concentrate and partially decontaminate the protein by adding sodium deoxycholate (DOC) and trichloroacetic acid (TCA) to the sample. Yet, this procedure alone has been insufficient for analysis of highly contaminated samples. In this report, we describe an improved method, the DOC-TCA-washing-BCA method, which is composed of the DOC-TCA precipitation and a subsequent aqueous washing that eliminates many interfering substances. The protein concentrations in samples containing even large amounts of interfering substances (e.g. various sugars and some detergents) were well quantitated by this method. The modifications described here have enabled us to perform rapid and efficient removal of many interfering substances that are commonly used in protein purification, and to allow proteins to be detected above 0.05 microgram and from a solution above 0.5 microgram/ml.

Deoxycholic Acid↗

PubMed1976

Insulin and glucagon degradation by the kidney. II. Characterization of the mechanisms at neutral pH.

Examination of insulin and glucagon degradation by rat kidney subcellular fractions revealed that most degrading activity was localized to the 100 000 X g pellet and 100 000 X g supernatant fractions. Further characterization of the degrading activities of the 100 000 X g pellet and supernatant suggested that three types of enzymatic activity were present at neutral pH. From the cytosol an enzyme with characteristics of the insulin glucagon protease of skeletal muscle was purified. This enzyme appeared to be responsible for insulin degradation by the kidney at physiological insulin concentrations. This enzyme also contributed to glucagon degradation but was not the most active mechanism for this. In the 100 000 X g pellet at least two separate enzymatic activities were present. One of these had properties consistent with those described for glutathione insulin transhydrogenase and appeared to be responsible for insulin degradation at high insulin concentration. The other enzyme was associated with the brush border and had properties consistent with the brush border neutral protease. This enzyme appeared responsible for glucagon degradation at both low and high substrate concentrations. An apparent marked synergism between the 100 000 X g pellet and the 100 000 X g supernatant was noted for insulin degradation at physiological insulin concentrations. Pellet glucagon-degrading activity and soluble insulin-degrading activity were necessary for this. The mechanism was found to be limited insulin degradation by the soluble enzyme resulting in both trichloroacetic acid-precipitable trichloroacetic acid-soluble fragments followed by further degradtion of the fragments by the glucagon-degrading enzyme resulting in an additional increase in trichloroacetic acid-soluble products.

Animals↗

PubMed1968

Pneumococcal C-substance, a ribitol teichoic acid containing choline phosphate.

1. Pneumococcal C-substance was isolated from the non-capsulated Pneumococcus 1-192R, A.T.C.C. 12213, by extraction with trichloroacetic acid solution followed by chromatography on DEAE-cellulose (HCO(3) (-) form). 2. The polymer contains 7.0% of phosphorus and 6.0% of nitrogen and is composed of phosphate, N-acetyl-d-galactosamine, d-glucose, N-acetyldiaminotrideoxyhexose, ribitol and choline in the molecular proportions 2:1:1:1:1:1. 3. After acid hydrolysis, d-galactosamine hydrochloride and galactosamine 6-phosphate were isolated in crystalline form and crystalline derivatives of d-glucose and anhydroribitol were obtained. A product of partial acid hydrolysis was provisionally characterized as 6'-O-phosphoryl-[O-beta-d-galactosaminyl-(1'-->6)-d-glucose]. 4. C-substance contains free amino groups accessible to attack by 1-fluoro-2,4-dinitrobenzene and nitrous acid. 5. Choline phosphate and ribitol phosphate are units in the polymer. 6. Treatment with hot alkali gave a fragment comprising phosphate, d-galactosamine, d-glucose, diaminotrideoxyhexose and ribitol in the molecular proportions 2:1:1:1:1. 7. After selective N-acetylation, the fragment contained one of its phosphate groups as a phosphomonoester and one as a phosphodiester, shown by potentiometric titration and by treatment with a phosphomonoesterase. 8. C-substance from seven other strains of Pneumococcus possesses a structure common to that described for the strain 1-192R. 9. Capsular materials from 26 different strains of Pneumococcus were analysed for suspected contamination by C-substance. In 19 cases the presence of C-substance with the normal structure was demonstrated, and in the remaining seven cases the contaminating C-substance was probably similarly constituted. 10. F-substance was isolated and the associated fatty acid material analysed.

Acids↗

PubMed1979

Re-evaluation of turbidimetry of proteins by use of aromatic sulfonic acids and chloroacetic acids.

From studies on 11 different proteins (including native albumin and albumin with reduced disulfide-bridges) treated with sulfosalicylic, 2-naphthalenesulfonic, toluenesulfonic, dichloroacetic, or trichloroacetic acids, we elucidate the interactions determining the resulting turbidities and other factors affecting turbidities, and we discuss the clinical utility of such turbidimetry. At least three interactions are important in determining turbidity: reduction of positive charges on the protein, hydrogen bonding of the non-ionized chloroacetic acids with the protein, and hydrophobic interaction of the aromatic sulfonic acids with albumin. Turbidity varies appreciably with the species of acid and protein, concentrations of acid, temperature, and standing time after acid is added. We conclude that this technique should be restricted to confirming proteinuria.

Albumins↗

PubMed2002

Chemical marker for ALS-inhibitor herbicides: 2-aminobutyric acid proportional in sub-lethal applications.

A chemical profiling technique for sub-lethal acetolactate synthase (ALS)-inhibitor herbicides (e.g., sulfonylureas, imidazolines, triazolopyrimidine sulfonanilides, and pyrimidyloxy salicylic) was developed using 2-aminobutyric acid, and was found to be directly proportional to application rates in field studies on two varieties of potato plants. An uncomplicated, benign-by-design analytical method for the determination of 2-aminobutyric acid in plant tissue was developed. The method is simple, fast, and automated, entailing a water-trichloroacetic acid extraction followed by precolumn on-line derivatization using o-phthalaldehyde (OPA) solution and liquid chromatographic analyses. Use of reagents and chlorinated organic solvents, and generation of waste, are minimized as compared to other ALS-inhibitor herbicide analytical techniques. Recoveries for a series of fortified plant tissues ranged from 82 to 103%. Two 20-day field trials on two potato varieties, Russet Burbank and Shepody, were conducted during the 2000 and 2001 growing seasons. The study demonstrated that the 2-aminobutyric acid method is an excellent, selective chemical marker technique for ALS-inhibitor herbicides for real world plant matrixes.

Acetolactate Synthase↗