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PubMed1991

Distribution of dietary limiting amino acid injected into the prepyriform cortex.

Diffusion or metabolism of the dietary limiting amino acid (DLAA) in the prepyriform cortex (PPC) may account for the time lag between injection of the DLAA into the PPC and the increase in intake of an amino acid-imbalanced diet. Results from the injection of [3H]Leu +/- [14C]Thr (DLAA) into the PPC indicated rapid (less than 15 min) and limited diffusion (85-90% of recovered label was less than or equal to 1 mm from the injection site). 3H and 14C decreased in the trichloroacetic acid (TCA)-soluble fraction and increased in the TCA-insoluble fraction during the first 1.5 h and remained constant in the TCA-insoluble fraction 1.5-6 h after injection. An increase (approximately 50%) in 3H in the TCA-insoluble fraction was found less than or equal to 30 min after injection of the DLAA. There was no affect of the DLAA on 3H in the TCA-soluble fraction. These results indicated that a change in metabolism within the PPC may be responsible for the delay in onset of the feeding response after injection of the DLAA into the PPC.

Amino Acids↗

PubMed1983

Bioluminescent assay for total bile acids in serum with use of bacterial luciferase.

This simple, rapid, sensitive kinetic bioluminescent method for the assay of bile acids in serum involves use of 3 alpha-hydroxysteroid dehydrogenase (EC 1.1.1.50) in combination with a new, commercially available NADH Monitoring Reagent (LKB-Wallac) containing a low activity of NADH:FMN-oxidoreductase and a high activity of bacterial luciferase. Interfering dehydrogenases in serum are inactivated in the test tube with trichloroacetic acid before the assay. The standard curve is linear for concentrations of bile acids up to about 300 mumol/L. With a sample volume of 20 microL, the detection limit is about 0.2 mumol/L. The within-run precision (CV) is about 10%, both at high and low concentrations of bile acids in serum. Correlation is good (r = 0.996) between results by this method and an enzymatic method based on spectrophotometry. However, the latter method is considerably less sensitive, and it is less precise at low concentrations of bile acids.

3-Hydroxysteroid Dehydrogenases↗

PubMed1972

Comparative studies of bile salts. A new type of bile salt from Arapaima gigas (Cuvier) (family Osteoglossidae).

1. Arapaima gigas bile salts were hydrolysed by alkali or cleaved with dioxan-trichloroacetic acid to give cholic acid, arapaimic acid, arapaimol-A and arapaimol-B. 2. I.r., n.m.r. and mass spectroscopy and [alpha](D) measurements indicated that arapaimic acid and arapaimol-A and -B are respectively 2alpha,3alpha,7alpha,12alpha-tetrahydroxy-5beta,25in-cholestan-26-oic acid, 5beta,25R-cholestane-2beta,3alpha,7alpha,12alpha,26-pentol and 5beta-cholestane-2beta,3alpha,7alpha,12alpha,26,27-hexol. 3. Partial synthesis of 2beta,3alpha,7alpha,12alpha-tetrahydroxy-5alpha- and -5beta-cholan-24-oic acid and their spectral examination fully confirmed these conclusions. 4. A. gigas bile salts show primitive features in that they comprise alcohol sulphates and a C(27) acid; they are also specialized in showing 2beta-hydroxylation.

Animals↗

PubMed1979

Haemagglutination by Staphylococcus saprophyticus and other staphylococcal species.

Staphylococcus saprophyticus was found to differ from Staphylococcus epidermidis and Staphylococcus aureus by its ability to agglutinate sheep erythrocytes. On testing 30 strains of each species, 28 strains of S. saprophyticus and one strain each of the other two species, caused agglutination. Twenty-eight of 30 strains of staphylococcus cohnii and Staphylococcus xylosis failed to cause haemagglutination. The haemagglutinating activity of S. saprophyticus, when using a 10 per cent bacterial suspension was demonstrated in dilutions of 1:2-1:32. It was reduced twofold, at most, when exposing the bacteria to 56 degrees C for 30 minutes, while no agglutination could be demonstrated after treatment for 10 minutes at 86 degrees C. No haemagglutination could be demonstrated after treatment of the bacteria with 5 per cent solution of trypsin. Treatment of S. saprophyticus with 0.1 M EDTA did not affect the haemagglutinating activity, whereas exposure of the bacteria to 10 per cent trichloroacetic acid reduced the activity. The haemagglutination was D-mannose-resistant, and it was inhibited by homologous rabbit antiserum. The agglutinates dispersed when heated at 45-56 degrees C for 30 minutes. A few of the strains of S. saprophyticus tested also agglutinated human, bovine, and guinea pig erythrocytes.

Animals↗

PubMed2006

Bayesian population analysis of a harmonized physiologically based pharmacokinetic model of trichloroethylene and its metabolites.

Bayesian population analysis of a harmonized physiologically based pharmacokinetic (PBPK) model for trichloroethylene (TCE) and its metabolites was performed. In the Bayesian framework, prior information about the PBPK model parameters is updated using experimental kinetic data to obtain posterior parameter estimates. Experimental kinetic data measured in mice, rats, and humans were available for this analysis, and the resulting posterior model predictions were in better agreement with the kinetic data than prior model predictions. Uncertainty in the prediction of the kinetics of TCE, trichloroacetic acid (TCA), and trichloroethanol (TCOH) was reduced, while the kinetics of other key metabolites dichloroacetic acid (DCA), chloral hydrate (CHL), and dichlorovinyl mercaptan (DCVSH) remain relatively uncertain due to sparse kinetic data for use in this analysis. To help focus future research to further reduce uncertainty in model predictions, a sensitivity analysis was conducted to help identify the parameters that have the greatest impact on various internal dose metric predictions. For application to a risk assessment for TCE, the model provides accurate estimates of TCE, TCA, and TCOH kinetics. This analysis provides an important step toward estimating uncertainty of dose-response relationships in noncancer and cancer risk assessment, improving the extrapolation of toxic TCE doses from experimental animals to humans.

Animals↗

PubMed1997

Perturbation of epidermal growth factor clearance after radioiodination and its implications.

The clearance of human epidermal growth factor (hEGF1-53) has been thought to be mediated mainly by a high-capacity receptor system, yet relatively low in vivo clearance rates (<10 mL/min/kg) and long terminal elimination half-lives (>120 min) have been observed in rats receiving the peptide that was iodinated by the oxidative chloramine-T (CT) method. We investigated if a mild, less oxidative iodination by the lactoperoxidase (Enzymobeads, EB) method, which is known to yield an iodinated peptide with receptor-binding equivalence, could produce a labeled peptide that behaves pharmacokinetically similar to the native material. For comparison, a parallel study was also conducted with EB-125I-hEGF1-48, which in its native form has a much reduced receptor binding activity due to the loss of the C-terminal pentapeptide. Plasma radioactivity concentrations were determined by trichloroacetic acid (TCA) precipitation and immunoprecipitation. Rats cleared unlabeled hEGF1-53 and hEGF1-48 markedly faster (CL(tot) > 120 mL/min/kg) than their radiolabeled counterparts. Approximately 96% of the hEGF1-53 dose was cleared during the initial phase (0-4 min), as opposed to only 5-14% for the iodinated peptide. Similar change was also observed for EB-125I-hEGF1-48 and CT-125I-hEGF1-53. The pharmacokinetic behavior of EB-125I-hEGF1-53 was, in fact, comparable to that of CT-125I-hEGF1-53. These observations indicate that receptor-binding equivalence does not have direct relationship with in vivo EGF clearance. Both iodination methods (oxidative CT and less oxidative EB) might have perturbed one or more steps in the cascade of ligand-receptor internalization and intracellular procession, which in turn modified the disposition of the peptides. In addition, the two independent precipitation techniques for the same peptide generated different kinetic outcomes. The overall experimental results suggest that it is unacceptable to use an iodinated form to characterize the disposition of peptides/proteins like EGF with a specific receptor system mediating its clearance.

Amino Acid Sequence↗

PubMed1980

Role of calcium ions in the formation and release of low-molecular-weight substances from optic nerve terminals.

Retinal proteins were labeled by intraocular injections of radioactive amino acids. Tissue slices of the superior colliculus (SC) were prepared 18-20 hr later, i.e., when the rapid phases of the axonal transport had reached the SC terminals. The effect of depolarizing pulses of high K and of Ca withdrawal on the scretion of radioactivity was studied in a perfusion system. The effluents were separated into a trichloroacetic acid (TCA) precipitable fraction and a TCA-soluble fraction. High K evoked a release of TCA-soluble radioactivity when [(3)H]glycine, [(3)H]leucine, or [(3)H]proline were used as protein precursors. Small changes occurred for TCA-precipitable fractions. The evoked release of radioactivity was Ca dependent and particularly prominent after labeling with [(3)H]glycine. Ca withdrawal increased the efflux of exogenous GABA, primary amines, and TCA-precipitable radioactivity but not of TCA-soluble radioactivity when normal media were used. The formation of TCA-soluble radioactivity was measured by incubating combined homogenates of SC and the lateral geniculate body (LGB), containing labeled proteins transported by the slow or rapid phase. The proteolytic activity was highly Ca dependent, for the rapidly transported proteins the half maximum was at approximately 0.1 mM Ca. The formation of TCA-soluble radioactivity was inhibited by p-chloromercuriphenylsulfonic acid (PCMS). Other divalent cations could not substitute for Ca. The rate of formation of TCA-soluble radioactivity and the influence of Ca ions was smaller when proteins of the slow phase were used as substrate.

Amino Acids↗

PubMed1983

Induction of protein and glycoprotein synthesis in rat submandibular glands by isoproterenol.

A family of proline-rich proteins which contain over 40% proline and a glycoprotein were isolated from submandibular glands of isoproterenol-treated rats by extraction with 10% trichloroacetic acid and fractionation of the acid-soluble portion on Bio-Gel A-1.5m. The proline-rich proteins were subsequently separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Proteins were detected by formaldehyde fixation and Coomassie staining. After elution from the gels, amino acid compositions were determined. The family of proline-rich proteins (about six) appears to be qualitatively identical with a family of proteins from parotid glands of isoproterenol-treated rats (Muenzer J., Bildstein, C., Gleason, M., and Carlson, D. M. (1979) J. Biol. Chem. 254, 5623-5628, 5629-5634), except for a substantial change in the relative amount of each protein. An acid-soluble glycoprotein (GP-158) was not detected in extracts of submandibular glands of normal rats, but GP-158 was highly induced by isoproterenol treatment. This glycoprotein has an apparent Mr = 158,000 as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The major amino acids were Asx, 13%; Glx, 18%; Pro, 29% and Gly, 11%. GP-158 contained about 37% carbohydrate, and its sugar composition on a molar basis was mannose, 3.0; galactose, 2.1; N-acetylglucosamine, 3.5; fucose, 1.2; and sialic acid (N-glycolyl(4-O-acetyl)neuraminic acid), 0.9. N-Acetylgalactosamine was not detected. A glycopeptide isolated from GP-158 had the same sugar composition as GP-158. The amino acid sequence of the glycopeptide was shown to be Asp-Gly-(Asn)-Gln-Thr-Gln-Pro-Arg-Pro-(Gly-Pro). Only the parotid and submandibular glands of rats responded in this dramatic fashion to isoproterenol. The isoproterenol-treated rat is considered an appropriate model system for studying the overall effects of catecholamine beta-agonists on gene expression in these secretory tissues.

Amino Acid Sequence↗

PubMed1995

Protein concentration by precipitation with pyrogallol red prior to electrophoresis.

The pyrogallol red protein assay (Clinical Chemistry 1986, 32, 1551-1554) is based upon formation of a blue protein-dye complex in the presence of molybdate under acidic conditions. However, centrifugation of the assay mixture results in loss of color yield and precipitation of the protein-dye complex which can be recovered and resolubilized to achieve protein concentration prior to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The method has been evaluated relative to trichloroacetic acid (TCA) precipitation for recovery and electrophoresis of commercial protein and peptide molecular weight markers. Precipitation with pyrogallol red-molybdate (PRM) gives better and more uniform recovery of both proteins and peptides as compared to TCA. The lower limit of PRM precipitation is similar to TCA and corresponds to 1 microgram protein per mL assay mixture. This is equivalent to 100 microL of 10 micrograms/mL protein using the standard protein assay or 1 microgram/mL protein using a modified assay incorporating a fivefold concentrate of the dye reagent. Application of the method is demonstrated by concentration of urinary proteins. The method is simple and economic and useful for conserving trace amounts of precious sample as it allows recovery of protein for electrophoresis following protein assay.

Chemical Precipitation↗

PubMed1990

Liberation of tryptic fragments from caseinomacropeptide of bovine kappa-casein involved in platelet function. Kinetic study.

Carbohydrate-free caseinomacropeptide (CMP) was purified from rennet-hydrolysed caseinate by trichloroacetic acid precipitation and DEAE-TSK Fractogel-650 ion-exchange chromatography. To study the liberation of 106-112, 106-116 and 113-116 fragments from carbohydrate-free CMP involved in platelet function, a quantitative study was made on the rate of hydrolysis of the three peptidic bonds that are susceptible to the action of trypsin. Data were obtained from reverse-phase (Ultrabase column) and cationic-exchange (Mono S column) h.p.l.c. On the basis of the disappearance of substrate, kcat. and Km were respectively 3.95 s-1 and 0.2 mM. The two 111-112 and 112-113 bonds were split according to similar kinetic parameters (kcat. = 1.97 s-1, Km = 0.2 mM) and much faster than the 116-117 bond. The difference in susceptibility of the bonds can probably be attributed to the nature of residues flanking the primary proteolytic sites rather than to their accessibility to the proteinase. On the basis of our results the 106-116 fragment cannot be formed.

Amino Acid Sequence↗

PubMed1997

Electron transfer between myoglobin and electrodes in thin films of phosphatidylcholines and dihexadecylphosphate.

Myoglobin (Mb) in thin films of phosphatidyl cholines (PC) or dihexadecyl phosphate (DHP) gave direct, reversible electron transfer between pyrolytic graphite electrodes and the heme Fe(III)/Fe(II) redox couple of the protein. PC films incorporated much more Mb than DHP films. A model assuming several classes of electroactive sites in the films on the electrode with a dispersion of standard potentials successfully fit square-wave voltammetric data at pulse heights > 50 mV. Electron transfer rate constants in PC and DHP films were significantly larger than for Mb in thin films of an insoluble cationic surfactant. The pH dependence of the formal potential of Mb in the PC films suggested that protonation, possibly inducing conformational change, accompanies electron transfer to MbFe(III) between pH 5 and 11. Mb in PC films was used for catalysis of the reduction of trichloroacetic acid.

Animals↗

PubMed1973

Association of nascent polypeptide with 30S ribosomal subunits.

1. Crude extracts of Escherichia coli were used to synthesize nascent peptides under the direction of endogenous mRNA and in the presence of radioactive amino acids. Analysis of such extracts by sucrose-gradient centrifugation in low Mg(2+) concentration has shown that after 2min of incubation approximately 14% of the total labelled protein recovered on the gradient, in association with whole ribosomes, sediments with 30S ribosomal subunits; this value rises to approximately 24% after 30min of incubation. The labelled protein associated with 30S ribosomal subunits is insoluble in hot trichloroacetic acid. 2. Similar results were also obtained in extracts that synthesized polypeptides under the direction of either of the synthetic polyribonucleotides poly(A) or poly(A,G,C,U). In contrast, however, analysis of crude extracts programmed in protein synthesis by poly(U) has indicated that under these conditions 30S ribosomal subunits have no associated polyphenylalanine; similarly there is little associated peptide after programming of extracts by poly(U,C).

Amino Acids↗

PubMed1987

Thyroid hormone inhibits fibronectin synthesis by cultured human skin fibroblasts.

Fibronectin (Fn) is a glycoprotein composed of two different subunits, each with a mol wt of approximately 230K. Fn is important for cell adhesion and for maintaining normal cell morphology. Recent in vivo studies suggested that thyroid hormone affects the plasma Fn level in man. The aim of this study was to determine whether T3 regulates the synthesis of Fn in cultured human skin fibroblasts. Skin fibroblasts obtained from seven normal subjects were grown in Minimum Essential Medium supplemented with 10% fetal calf serum. After reaching confluence, the cells were exposed for 3 days to the same medium in which fetal calf serum was replaced by 10% thyroidectomized bovine serum without or with added T3. At the end of this period, the cultures were incubated with [35S]methionine (95 microCi/dish) for 4 h before harvesting. Cell lysates and corresponding media were combined, and 35S incorporation into total protein and Fn was determined by trichloroacetic acid precipitation and immunoprecipitation with antihuman Fn immunoglobulin, respectively. Analysis of the immunoprecipitated material by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that most of the 35S activity migrated as a 230K band which was displaced by excess unlabeled Fn. Addition of T3 did not affect trichloroacetic acid-precipitable 35S activity but decreased the 35S activity precipitated with anti-Fn in a dose-dependent manner. While addition of 10(-10) M T3 to the medium had no effect, 35S incorporation into Fn was inhibited by 22.5 +/- 7.4% (mean +/- SD) with 10(-9) M T3 (free T3, 6 X 10(-12) M) and by 31.3 +/- 5.8% with 10(-7) M T3. To assess whether the inhibition of Fn accumulation by T3 was due to suppression of Fn synthesis or enhanced Fn degradation, cells were labeled for 4 h with [35S]methionine and chased for another 4 h with excess unlabeled methionine. T3 had no effect on the rate of decline of [35S]Fn during the chase. We conclude that physiologic T3 concentrations inhibit the synthesis of Fn in normal human fibroblasts. This effect provides a new method to study the action of thyroid hormone which may prove useful in the tissue diagnosis of resistance to thyroid hormone.

Adult↗

PubMed2004

Voltammetric studies of hemoglobin-coated polystyrene latex bead films on pyrolytic graphite electrodes.

A novel hemoglobin (Hb)-coated polystyrene (PS) latex bead film was deposited on pyrolytic graphite (PG) electrode surface. In the first step, positively charged Hb molecules in pH 5.0 buffers were adsorbed on the surface of negatively charged, 500 nm diameter PS latex beads bearing sulfate groups by electrostatic interaction. The aqueous dispersion of Hb-coated PS particles was then deposited on the surface of PG electrodes and, after evaporation of the solvent, Hb-PS films were formed. The Hb-PS film electrodes exhibited a pair of well-defined, quasi-reversible cyclic voltammetric (CV) peaks at about -0.36 V vs. SCE in pH 7.0 buffers, characteristic of Hb heme Fe(III)/Fe(II) redox couples. Positions of Soret absorption band of Hb-PS films suggest that Hb retains its near-native structure in the films in its dry form and in solution at medium pH. The Hb in PS films was also acted as a catalyst to catalyze electrochemical reduction of various substrates such as trichloroacetic acid (TCA), nitrite, oxygen and hydrogen peroxide.

Animals↗

PubMed2006

Gold nanoparticle-assisted protein enrichment and electroelution for biological samples containing low protein concentration--a prelude of gel electrophoresis.

Protein enrichment is essential for biological samples that contain low protein concentrations, especially for proteomic studies that require sufficient quantities for subsequent MS analysis. Traditional precipitation methods, however, are limited in the sample volume and protein concentration required to cause efficient precipitations. We showed that gold nanoparticles (Au-NPs) can be easily applied to concentrate proteins from more than 15 mL of human urine, in which the total protein concentration is less than 1.4 ppm. Moreover, Au-NP-aggregated proteins can be directly applied to gel electrophoresis for Au-NP-protein dissociation followed by free protein separation as well as for the subsequent in-gel digestion and protein identification by mass spectrometry. We compared this method with trichloroacetic acid (TCA) precipitation method, one of the most common precipitation methods, and TCA method showed no enrichment effect for protein samples with large volumes (>2 mL) or with low protein concentrations (4 ppm). Therefore, Au-NP aggregation is not only a simple and efficient method for enriching a broad range of proteins, it is also particularly useful for concentrating proteins from a relatively large volume of dilute biological fluids, under which TCA method is ineffective.

Amino Acid Sequence↗

PubMed1967

Studies on the proteolytic activity of gamma-globulin preparations.

1. The proteolytic activities of several gamma-globulin preparations were tested. These included sulphate-precipitated human and bovine preparations and human and bovine Cohn fraction II preparations as well as purified gamma-globulin preparations. Up to 14mg. of diffusible peptides and glycopeptides/g. of gamma-globulin was liberated after dialysis and up to 10mg. of peptides/g. after incubation and trichloroacetic acid precipitation, as products of the degradation process in incubated gamma-globulin. 2. in-Aminohexanoic acid and p-chloromercuribenzoic acid, as well as heating at 60 degrees for 40min., were shown to inhibit strongly these proteolytic activities. Streptokinase was shown to activate strongly the proteolytic activity of all the human preparations (sulphate-precipitated, Cohn fraction II, and purified gamma-globulin). 3. Two distinct pH optima were shown for human and bovine gamma-globulin preparations: one at pH8, the other at pH3.8 (the latter activity could be demonstrated only in the presence of cysteine). 4. Both (131)I-labelled human Cohn fraction II and bovine fibrinogen were attacked by a sulphate-precipitated preparation of gamma-globulin. Of the synthetic substrates tested toluene-p-sulphonyl-l-arginine methyl ester was hydrolysed by both the sulphate-precipitated and Cohn fraction II preparations, as was benzoyl-l-arginine amide at pH5, but only in the presence of cysteine. 5. These data are interpreted to indicate that at least two enzymes are present in gamma-globulin preparations, one being similar to the plasmin system, the other similar to cathepsin B.

Acids↗

PubMed1999

Physiologically based pharmacokinetic modeling of inhaled trichloroethylene and its oxidative metabolites in B6C3F1 mice.

A physiologically based pharmacokinetic (PBPK) model for inhaled trichloroethylene (TCE) was developed for B6C3F1 mice. Submodels described four P450-mediated metabolites of TCE, which included chloral hydrate (CH), free and glucuronide-bound trichloroethanol (TCOH-f and TCOH-b), trichloroacetic acid (TCA), and dichloroacetic acid (DCA). Inhalation time course studies were carried out for calibration of the model by exposing mice to TCE vapor concentrations of either 100 or 600 ppm for 4 h. At several time points, mice were euthanized and blood, liver, kidney, lung, and fat were collected and analyzed for TCE and its oxidative metabolites. Peak blood TCE concentrations were 0.86 and 7.32 microgram/mL, respectively, in mice exposed to 100 and 600 ppm TCE. The model overpredicted the mixed venous blood and tissue concentrations of TCE for mice of both exposure groups. Fractional absorption of inhaled TCE was proposed to explain the discrepancy between the model predictions and the TCE blood time course data. When fractional absorption (53%) of inhaled TCE was incorporated into the model, a comprehensive description of the uptake, distribution, and clearance of TCE in the blood was obtained. Fractional uptake of inhaled TCE was further verified by collecting TCE in exhaled breath following a 4-h constant concentration exposure to TCE and validation was provided by testing the model against TCE blood concentrations from an independent data set. The submodels adequately simulated the distribution and clearance kinetics of CH and TCOH-f in blood and the lungs, TCOH-b in the blood, and TCA and DCA, which were respectively detected for up to 43 and 14 h postexposure in blood and livers of mice exposed to 600 ppm TCE. This is the first extensive tissue time course study of the major metabolites of TCE following an inhalation exposure to TCE and the PBPK model predictions were in good general agreement with the observed kinetics of the oxidative metabolites formed in mice exposed to TCE concentrations of 100 and 600 ppm.

Adipose Tissue↗

PubMed2006

Comparison of three methods for enamel protein extraction in different developmental phases of rat lower incisors.

Protein extraction methods [urea, trichloroacetic acid (TCA), and acetic acid] were compared for protein recovery from rat incisor developing enamel in the S phase (intermediate/late secretion), M1 phase (early maturation), M2 phase (intermediate maturation), and M3 phase (final maturation). We compared the protein recoveries with the percentage of enamel matrix dry weight burnt off by incineration. Our results indicate that TCA and urea were equally efficient for the extraction of S-stage proteins (85% and 90% recovery, respectively), while urea was the best for M1-stage proteins (92% recovery), and TCA the best for M2-stage (99% recovery) and M3-stage (60% recovery) proteins. The other methods yielded less than 30% recovery in comparison to incineration for M2 and M3 stages. The fact that urea extraction works well in the S and M1 stages and not thereafter is probably related to the changes in the proteins during enamel development and the amount of mineral that needs to be dissolved. TCA is the single method that effectively recovered proteins from all developmental stages of the rat incisor enamel.

Acetic Acid↗