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PubMed1971

Localization and solubilization of colicin receptors.

Envelope fractions isolated from Escherichia coli K-12 C600 and from colicin-resistant and colicin-tolerant (Tol II) mutants derived from this strain were separated on sucrose gradients into cell wall-enriched and cytoplasmic membrane-enriched fractions. These fractions were tested for their ability to neutralize colicins of the E and K groups. Neutralization activity was found in the cell wall-enriched fraction from the parent and the Tol II mutant but was absent from all fractions from the resistant mutant. This was also tested with several other E. coli strains. In all cases, sensitive strains contained the neutralization activity, whereas resistant strains did not. The neutralization activity was solubilized from cell walls or cell envelopes of sensitive or Tol II strains by extraction at room temperature with Triton X-100 plus ethylenediaminetetraacetic acid. The solubilized activity was precipitated by 20% ammonium sulfate, 70% ethanol, or 10% trichloroacetic acid. The activity was destroyed by treatment of the solubilized preparation with trypsin or periodate. These results suggest that this colicin-neutralization activity is due to the presence of specific receptors localized in the cell wall and that intact protein and a carbohydrate are required for this receptor to bind colicin.

Ammonium Sulfate↗

PubMed1996

Formation of dichloroacetic acid by rat and mouse gut microflora, an in vitro study.

Metabolism of trichloroethylene (TRI) and its major metabolite, trichloroacetic acid (TCA), by gut content and gut microflora cultures was studied to gain an insight into the role of enterohepatic circulation in TRI metabolism. TRI and TCA were incubated anaerobically with rat and mouse cecal contents and TCA was additionally incubated anaerobically and aerobically with microflora cultures from mice. Although TRI was not metabolized by rat or mouse cecal contents. TCA was metabolized to dichloroacetic acid (DCA) by cecal contents. DCA formation in microflora cultures was dependent on initial TCA concentration, duration of incubation, and initial bacterial number. DCA was not observed in aerobic cultures exposed to TCA. These results suggest that strict anaerobic microorganisms of the gut may partly be responsible for dechlorination of TCA to DCA.

Aerobiosis↗

PubMed1988

Defective lysosomal release of glycoprotein-derived sialic acid in fibroblasts from patients with sialic acid storage disease.

Fibroblasts from patients with sialic acid storage disease (SASD), sialidosis, mucolipidosis II, and from normal controls, were incubated in the presence of the glycoprotein fetuin that was tritium-labelled in its sialic acid residues by the periodate/[3H]borohydride reduction method, and the fate of the intracellular radioactive sialic acid (C7-sialic acid) followed in pulse-chase experiments. The model glycoprotein was readily endocytosed and degraded, more than 90% of the radioactivity being trichloroacetic acid (TCA)-soluble after 4 days of incubation. In all of the patients' fibroblasts, there was an increased accumulation of TCA-soluble radioactivity and, upon chase, a much lower rate of elimination than in normal controls. Gel chromatography of the material from the chase experiment showed that, in normal cells, most of the radioactivity at zero time behaved as free C7-sialic acid. This, as well as material of larger size (sialyloligosaccharides), was very much diminished by 48 h. In cells from two patients with SASD, there were large peaks both in the sialic acid and oligosaccharide positions; whereas the oligosaccharides were somewhat decreased by the end of the chase period, the sialic acid was essentially unchanged. In sialidosis fibroblasts, the radioactive material consisted of oligosaccharides, but very little C7-sialic acid; the elimination of the oligosaccharides was retarded. In normal cells, about 80% of the radioactivity released into the medium after 48 h chase behaved as free C7-sialic acid upon gel chromatography and t.l.c. Subcellular fractionation in Percoll gradients showed that the radioactive C7-sialic acid remaining in normal cells after 48 h of chase was mainly localized in the cytosol. In SASD cells, on the other hand, it was associated with lysosomal fractions which, unexpectedly, exhibited an abnormally low density. Our findings demonstrate that SASD fibroblasts degrade the sialoglycoprotein but, unlike normal cells, accumulate the liberated C7-sialic acid along with sialyloligosaccharides in their lysosomes. The results therefore support the concept of a defective transport system for sialic acid in the lysosomal membrane of patients with SASD.

Biological Transport↗

PubMed1998

Simple, rapid and sensitive determination of protionamide in human serum by high-performance liquid chromatography.

A simple high-performance liquid chromatography method has been developed that allows the sensitive determination of protionamide (2-n-propyl-pyridine-4-carboxylic acid thioamide, PTH) in human serum. After pretreatment of the serum with trichloroacetic acid (TCA) and centrifugation the supernatants were neutralized using NaHCO3. PTH was separated on a Kromasil 100 C4 column (acetonitrile-sodium tetraborate buffer pH 8-dibutylamine) and determined photometrically at 291 nm. The lower limit of quantification for 300 microl serum precipitated with 60 microl TCA and injection of 50 microl was 27 microg/l and linearity was observed up to 15 mg/l.

Antitubercular Agents↗

PubMed2001

Dermal peels.

Dermal chemical peeling is a very satisfying procedure for patients and physicians alike. Although not providing the ablation of deep wrinkles and scars that dermabrasion and laser procedures may accomplish, trichloroacetic acid peels usually result in few complications and rapid recovery. Patients can usually expect photographic improvement in their skin. The results are usually long lasting, and most patients do not need to repeat dermal peels for at least 2 years. Of all resurfacing procedures, dermal peeling provides the best benefit-to-risk ratio.

Chemexfoliation↗

PubMed1996

Medium-depth chemical peeling.

Trichloroacetic acid (TCA) alone or in combination with other agents is the mainstay of medium-depth chemical peels. Indications for medium-depth chemical peels include both medical conditions, such as diffuse photodamage with contiguous actinic keratoses, and cosmetic conditions, such as the aging face and solar lentiginosis. Medium-depth chemical peeling with TCA is relatively simple and is associated with a favorable risk/benefit ratio. However, proper patient selection, with attention to both medical and psychological factors, requires significant experience. The histological basis of the rejuvenating effects of TCA peels is well established, with a consistent correlation between wound depth and TCA concentration. The clinical effects of medium-depth chemical peels are generally gratifying for both patient and physician.

Administration, Cutaneous↗

PubMed1972

A polymer of N-acetylglucosamine 1-phosphate in the wall of Staphylococcus lactis 2102.

1. Walls of Staphylococcus lactis 2102 contain about 40% of a phosphorylated polysaccharide, which was isolated by extraction with cold trichloroacetic acid, with dilute NaOH, and also by digestion with a Flavobacterium peptidase. 2. The purified polymer contained equimolar proportions of N-acetylglucosamine and phosphate as its sole constituents and was readily hydrolysed under gentle acidic conditions to N-acetylglucosamine 6-phosphate. 3. Studies on the intact polymer showed that it is linear and that adjacent acetamido sugar units are joined by phosphodiester bonds between their 1- and 6-positions, the glycosidic linkages having the alpha-configuration. This polymer is thus the simplest of the known microbial wall polymers possessing sugar 1-phosphate linkages. 4. Alkali degradation of the extracted polymer proceeds predominantly in a stepwise manner from the reducing end, but evidence was obtained for the direct hydrolysis of some of the inter-unit phosphodiester groups.

Acids↗

PubMed2002

Medium-depth chemical peels in the treatment of acne scars in dark-skinned individuals.

BACKGROUND: Multiple modalities are available for treating acne scars, one of which is chemical peeling. OBJECTIVE: To evaluate the efficacy of medium-depth peels in the treatment of acne scars. METHODS: A total of 15 patients (14 women and 1 man) were seen between November 1998 and March 2000. A medium-depth chemical peel was performed. The peel was performed using a combination of Jessner's solution followed by the application of 35% trichloroacetic acid (TCA). The mean age of patients who entered the study was 28 years. A total of 42 peeling sessions were performed: 13 patients had the full three-session regiment, 1 patient had two sessions, and 1 had only one session. RESULTS: Patients in our study had two forms of acne scars, the atrophic saucer or crater-like form and the pitted (ice-pick) form. Improvement occurred in all except one of our patients. Significant improvement (greater than 75% clearance of lesions) occurred in 1 patient (6.6%), moderate improvement (51-75% clearance) in 8 patients (53.3%), mild improvement (26-50% clearance) in 4 patients (26.6%), minimal improvement (1-25% clearance) in 1 patient (6.6%), and no response in 1 patient (6.6%). All patients had different combinations of the above two forms. Four patients (26.6%) had mainly pitted scars and deep atrophic scars. The clinical response in those patients was moderate, mild, minimal, and no response, respectively. The remainder of our patients had mainly atrophic scars of moderate depth. Nine patients (73.4%) suffered from transient postinflammatory hyperpigmentation. In two of them it was preceded by erythema that lasted for more than 1 month. All patients were free of noticeable pigmentation 3 months after the final peel. Patients in whom hyperpigmentation did not develop were of light brown complexion. CONCLUSION: We conclude that medium-depth chemical peel is a safe and effective method of treating acne scars even in patients with dark complexion.

Acne Vulgaris↗

PubMed1976

Quantitation of antibiotics using high-pressure liquid chromatography: tetracycline.

A method for quantitative determination of tetracycline in serum, using high-pressure liquid chromatography, is reported. After extraction of the drug from serum, using methanol-trichloroacetic acid solution, tetracycline was separated by reverse-phase chromatography. Quantitation of tetracycline was based on a linear relationship between peak heights in the chromatograms and known concentrations of the drug in the original serum samples. Serum tetracycline concentrations as low as 0.3 mug/ml could be accurately measured. Serum samples obtained after a single intravenous injection of tetracycline to three human volunteers and six dogs were assayed by microbiological and chemical assays. Correlation coefficients of 0.95 and 0.97, respectively, were found. This chemical method is rapid (less than 30 min), accurate, sensitive, and reproducible, and it seems feasible for routine clinical use.

Biological Assay↗

PubMed2000

Proteolysis in Manchego-type cheese salted by brine vacuum impregnation.

A new salting procedure based on the brine vacuum impregnation of porous products was tested on Manchego-type cheese and compared with conventional brine immersion. Its effect on cheese proteolysis throughout a 90-d ripening period was determined. Three cheese regions were evaluated (the rind, the middle, and the internal regions). The parameters analyzed were total N, water-soluble N, soluble N in trichloroacetic acid and soluble N in phosphotungstic acid by using the Kjeldahl method, casein profile by urea-PAGE, and peptide profile of the water soluble nitrogen extract by reverse-phase HPLC. Free amino acid formation was monitored with a spectrophotometric method by using a Cd-ninhydrin reagent. Globally, proteolysis was significantly affected by ripening stage (increasing throughout all the maturation period studied) and cheese region (rind showed a proteolysis pattern different from the middle and internal regions). The salting procedure only affected cheese proteolysis in the rind, whereas conventional brine-salted cheeses showed lower proteolysis than vacuum-impregnated cheeses.

Amino Acids↗

PubMed1988

Conversion of biosynthetic human proinsulin to partially cleaved intermediates by collagenase proteinases adsorbed to isolated rat adipocytes.

Studies of the biological activity of proinsulin have resulted in widely varying conclusions. Relative to insulin, the biological activity of proinsulin has been reported from less than 1% to almost 20%. Many of the assays in vitro for the biological potency of proinsulin have utilized isolated rat adipocytes. To examine further the interaction of proinsulin with rat adipocytes, we prepared specifically-labelled proinsulin isomers that were iodinated on tyrosine residues corresponding to the A14, A19, B16 or B26 residue of insulin. These were incubated with rat adipocytes and their metabolism was examined by trichloroacetic acid precipitation, by Sephadex G-50 chromatography, and by h.p.l.c. chromatography. By trichloroacetic acid-precipitation assay, there was little or no proinsulin degradation. By G-50 chromatography and subsequent h.p.l.c. analysis, however, we found that the labelled proinsulin isomers were converted rapidly and almost completely to materials which eluted differently on h.p.l.c. from intact proinsulin. This conversion was due primarily to proteolytic activity which adsorbed to the fat cells from the crude collagenase used to isolate the cells. Two primary conversion intermediates were found: one with a cleavage at residues 23-24 of proinsulin (the B-chain region of insulin), and one at residues 55-56 in the connecting peptide region. These intermediates had receptor binding properties equivalent to or less than intact proinsulin. These findings show that isolated fat cells can degrade proinsulin to intermediates due to their contamination with proteolytic activity from the collagenase used in their preparation. Thus the previously reported range in biological activities of proinsulin in fat cells may have arisen from such protease contamination. Finally, the present findings demonstrate that a sensitive assay for degradation of hormones is required to examine biological activities in isolated cells.

Adipose Tissue↗

PubMed1996

The TCA Masque. A new cream formulation used alone and in combination with Jessner's solution.

BACKGROUND: Traditional trichloroacetic acid (TCA) peel results are often unpredictable. "Hot spots," delayed healing, and scarring are not uncommon. OBJECTIVE: To reveal how the TCA Masque, used alone or in combination with Jessner's solution, helps minimize some of these problems while retaining efficacy. RESULTS: The masque's ease of application and its easily visualized one-time application have produced effective, safe, and predictable outcomes. The skin peels uniformly. CONCLUSIONS: The masque is also versatile since it is available in 11% and 16.9% strengths and can be applied thickly or spread thinly on the face, neck, arms, etc. When used alone, dyschromia and fine wrinkles are eliminated; the skin appears freshened. When used in combination with Jessner's and 16.9% TCA Masque a medium depth peel is achieved.

Chemexfoliation↗

PubMed1998

Studies on immunodiagnosis of dracunculiasis. II. Search for circulating antigens.

Sera from individuals living in a dracunculiasis endemic area of northern Ghana were examined for circulating Dracunculus medinensis antigens by applying protocols previously developed for detection of circulating antigens in other helminth infections. Antisera from rabbits immunised with homogenized first stage D. medinensis larvae were used for antigen capture and detection in three different forms, namely non-treated, biotinylated and horseradish peroxidase (HRP)-labelled. Three different preparations of human sera were examined, namely non-treated, pre-treated with polyethylene glycol/ethylenediaminetetra-acetic acid (PEG/EDTA) for analysis of precipitated immune complexes, and pre-treated with trichloroacetic acid (TCA) for analysis of isolated glycoproteins. In both SDS-PAGE/Western blotting and ELISA, significant reactivity was observed between non-treated and treated rabbit-antisera on the one hand and non-treated and treated human sera on the other. However, no significant response differences were observed between sera obtained from individuals with dracunculiasis and non-endemic controls. The reasons are analysed and possible explanations presented. The study provided no evidence that D. medinensis-specific circulating antigens, detectable by relatively simple means, occur in infected individuals.

Adolescent↗

PubMed1989

Species and strain sensitivity to the induction of peroxisome proliferation by chloroacetic acids.

B6C3F1 mice and Sprague-Dawley rats were provided drinking water containing 6-31 mM (1-5 g/liter) trichloroacetic acid (TCA), 8-39 mM (1-5 g/liter) dichloroacetic acid (DCA), or 11-32 mM (1-3 g/liter) monochloroacetic acid (MCA) for 14 days. TCA and DCA, but not MCA, increased the mouse relative liver weight in a dose-dependent manner. Rat liver weights were not altered by TCA or DCA treatment, but were depressed by MCA. Hepatic peroxisome proliferation was demonstrated by (1) increased palmitoyl-CoA oxidase and carnitine acetyl transferase activities, (2) appearance of a peroxisome proliferation-associated protein, and (3) morphometric analysis of electron micrographs. Mouse peroxisome proliferation was enhanced in a dose-dependent manner by both TCA and DCA, but only the high DCA concentration (39 mM) increased rat liver peroxisome proliferation. MCA was ineffective in both species. Three other mouse strains (Swiss-Webster, C3H, and C57BL/6) and two strains of rat (F344 and Osborne-Mendel) were examined for sensitivity to TCA. TCA (12 and 31 mM) effectively enhanced peroxisome proliferation in all mouse strains, especially the C57BL/6. A more modest enhancement in the Osborne-Mendel (288%) and F344 rat (167%) was seen. Dosing F344 rats with 200 mg/kg TCA in water or corn oil for 10 days increased peroxisome proliferation 179 and 278%, respectively, above the vehicle controls. These studies demonstrate that the mouse is more sensitive than the rat with respect to the enhancement of liver peroxisome proliferation by TCA and DCA and suggest that if peroxisome proliferation is critical for the induction of hepatic cancer by TCA and DCA, then the rat should be less sensitive or refractory to tumor induction.

Acetates↗

PubMed1971

Bacteriophage T4 inhibits colicin E2-induced degradation of Escherichia coli deoxyribonucleic acid. I. Protein synthesis-dependent inhibition.

The deoxyribonucleic acid (DNA) of Escherichia coli B is converted by colicin E2 to products soluble in cold trichloroacetic acid; we show that this DNA degradation (hereafter termed solubilization) is subject to inhibition by infection with bacteriophage T4. At least two modes of inhibition may be differentiated on the basis of their sensitivity to chloramphenicol. The following observations on the inhibition of E2 by phage T4 in the absence of chloramphenicol are described: (i) Simultaneous addition to E. coli B of E2 and a phage mutated in genes 42, 46, and 47 results in a virtually complete block of the DNA solubilization normally induced by E2; the mutation in gene 42 prevents phage DNA synthesis, and the mutations in genes 46 and 47 block a late stage of phage-induced solubilization of host DNA. (ii) This triple mutant inhibits equally well when added at any time during the E2-induced solubilization. (iii) Simultaneous addition to E. coli B of E2 and a phage mutated only in gene 42 results in extensive DNA solubilization, but the amount of residual acid-insoluble DNA (20 to 25%) is more characteristic of phage infection than of E2 addition (5% or less). (iv) denA mutants of phage T4 are blocked in an early stage (endonuclease II) of degradation of host DNA; when E2 and a phage mutated in both genes 42 and denA are added to E. coli B, extensive solubilization of DNA occurs with a pattern identical to that observed upon simultaneous addition of E2 and the gene 42 mutant. (v) However, delaying E2 addition for 10 min after infection by this double mutant allows the phage to develop considerable inhibition of E2. (vi) Adsorption of E2 to E. coli B is not impaired by infection with phage mutated in genes 42, 46, and 47. In the presence of chloramphenicol, the inhibition of E2 by the triple-mutant (genes 42, 46, and 47) still occurs, but to a lesser extent.

Adsorption↗

PubMed1974

Isolation of an acidic surface antigen from a conventional strain of Staphylococcus aureus.

Staphylococcus aureus strain 7007, a prototype isolated from a hospital burn unit, was shown to exhibit a significant degree of resistance to ingestion by mouse polymorphonuclear leukocytes. An acidic surface antigen was isolated from strain 7007 by a combination of 10% trichloroacetic acid extraction, ion-exchange chromatography, and gel filtration. Chemical analysis indicated that the surface antigen consists of an unknown aminouronic acid and an amino sugar. Immunochemical analysis suggested that the 7007 antigen is a common feature of all the strains collected from the burn unit. No cross-reactivity was observed between the carbohydrate preparations of various hospital staphylococcal strains and the 7007 heteropolymer. These results suggested the possibility that the surface antigen of strain 7007 represents a strain- or type-specific antigen.

Agglutination Tests↗

PubMed1985

Method for determining the lung burden of talc in rats and mice after inhalation exposure to talc aerosols.

A method has been developed to quantitate talc lung burdens in rats and mice after inhalation exposure to talc aerosols. The method is based on acid-insoluble magnesium (Mg) determination by flame atomic absorption. Precipitating protein from homogenates of lungs of unexposed rodents with 5% perchloric acid and washing with 5% trichloroacetic acid removed the soluble and naturally occurring Mg. This resulted in residual Mg content averaging 0.43 micrograms Mg per g lung in rats and less than 0.1 microgram Mg per g lung in mice for young rodents less than 12 weeks old. Rodents 12-18 months old had residual mean (+/- SD) Mg contents of 3.4 +/- 2.0 micrograms Mg per g rat lung (n = 17) and 6.5 +/- 2.9 micrograms Mg per g mouse lung (n = 12). Thus, the background residual acid-insoluble Mg content in rodent lungs appears to increase with age. Negligible quantities of Mg were extracted directly from the talc treated by these procedures. Adding 50-2000 micrograms talc to lungs from unexposed rodents, followed by the sample treatment, gave mean (+/- SD) Mg recoveries of 89 +/- 12% (n = 19) for rat lungs and 96 +/- 26% (n = 15) for mouse lungs. The lung burden of talc in rodents exposed to talc aerosols for 6 h per day, 5 days per week for 4 weeks was determined. Mean lung burdens in rats were 77, 187, and 806 micrograms talc per g lung (n = 10) for exposures at 2.3, 4.3, and 17 mg talc m-3, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)

Aerosols↗

PubMed1984

Metabolism of the alpha-amino nitrogen of glutamine in rat lens.

Rat lenses were cultured 4-24 h at 37 degrees C in balance salt medium containing 5 mM [15N]-(amino)-glutamine or 5 mM [15N]-glutamate. Free amino acids were extracted with 6% trichloroacetic acid containing alpha-aminoisobutyrate as an internal standard, and trifluoroacetyl-n-butyl (TAB) derivatives were prepared. Amino acids were quantified by gas chromatography, and 15N enrichment in amino groups of several lenticular free amino acids was determined by mass spectrometry. Culture of lenses with [15N]-(amino)-glutamine resulted in more rapid [15N]-labeling of the lenticular glutamate-glutamine pool than with [15N]-glutamate. The [15N]-(amino)-glutamine entered the lenses, and within 4 hr the lenticular glutamine-glutamate pool contained 70% amino-[15N] and had more than doubled in concentration. In contrast, [15N]-glutamate entered the lenses more slowly and lenticular glutamate-glutamine reached 30% 15N in 4 hr and 60% in 24 hr, with little change in concentration. The more rapid entry of [15N]-(amino)-glutamine resulted in more labeling of other amino acids than with [15N]-glutamate. For example, after 8 hr of culture, the lenses in [15N]-(amino)-glutamine contained a % 15N enrichment of 31 in alanine, 8 in glycine, 44 in proline, 24 in serine, 62 in aspartate-asparagine, and 78 in glutamate-glutamine, compared to values of 15, 5, 20, 13, 38, and 37 respectively for the lenses in [15N]-glutamate. The results indicate that in rat lenses the two-step process of glutamine transport and deamidation is more rapid than direct transport of glutamate. Lenses cultured with glutamine released sufficient ammonia into the culture medium to account for most of the added glutamine amido nitrogen. The data indicate that the amido nitrogen of glutamine is not utilized by the lens, but is lost to the surrounding medium. In contrast, the alpha-amino nitrogen can serve as a source of nitrogen for many important pathways of lens amino acid metabolism.

Amino Acids↗