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PubMed2003

Generation of free radicals and/or active oxygen by light or laser irradiation of hydrogen peroxide or sodium hypochlorite.

Generation of free radical and/or active oxygen by light or laser irradiation of hydrogen peroxide (H2O2) or sodium hypochlorite (NaClO), which have been used for tooth whitening or root canal irrigation, was investigated using electron spin resonance spectroscopy combined with a spin-trapping technique. When H2O2 was exposed to light or laser radiation, the amount of hydroxyl radical generated changed according to the concentration of H2O2 and irradiation time. The amount of 5,5-dimethyl-1-pyrrolidone-(2)-oxyl-(1) (DMPO-X) also changed in accordance with irradiation time. The amounts of hydroxyl radical generated from H2O2 after irradiation were in the order: plasma lamp > halogen lamp > He-Ne laser > Yellow He-Ne laser. On the other hand, the amounts of DMPO-X generated from NaClO after irradiation were in the order: plasma lamp > Yellow He-Ne laser > halogen lamp > He-Ne laser.

Cyclic N-Oxides↗
PubMed2000

An in vivo comparison of the kinetics of protein and lipid deposition on group II and group IV frequent-replacement contact lenses.

PURPOSE: To investigate the degree and rate of deposition of protein and lipid on FDA group II and group IV contact lens materials over a period of up to 28 days of wear. METHODS: Twenty-two subjects wore a group IV lens (Acuvue) and a group II lens (Soflens 66) in a randomized, cross-over study. The lenses were randomly worn for periods between 1 and 28 days and then collected for laboratory-based deposition analysis. RESULTS: The group II lenses revealed an increased degree of lipoidal spoilage (p < 0.0001) and the group IV lenses exhibited increased protein spoilage (p < 0.0001). Surface protein for both materials reached a maximum after 1 day and did not increase over the 4-week wearing period (p = NS). Total protein for group IV lenses reached a maximum between 1 and 7 days and then reached a plateau, with no further increase occurring (p = NS), whereas total protein accumulation on the group II lens continued to increase across all time periods (p < 0.05). Lipid deposition on the group IV lens was maximal after 1 day and increased no further (p = NS), whereas lipid deposition on the group II material monotonously increased and progressively built-up over the 4 weeks of wear (p < 0.0001). CONCLUSIONS: The kinetics of contact lens deposition is mediated by the chemical structure of the contact lens material under consideration. Protein deposition occurs rapidly with group IV materials before reaching a maximum, whereas N-vinyl pyrrolidone-containing group II materials progressively accumulate protein and lipid deposits, with no plateau occurring.

Adult↗
PubMed1992

The Isolation of Actin from Pea Roots by DNase I Affinity Chromatography.

Native actin can be isolated from pea (Pisum sativum L.) roots by DNase I affinity chromatography, but the resulting yields and quality of actin are variable. By use of two assays for actin, a DNase I inhibition assay and a gel scanning assay, we identified several factors that increased actin yield. ATP is required for the actin in crude pea root extracts to bind to immobilized DNase I. Low amounts of ATP are hydrolyzed rapidly by an endogenous ATPase in the extract, and the actin then irreversibly loses the ability to bind to DNase I. High ATP concentrations (5-10 mm) or inhibition of the ATPase (with 10 mm pyrophosphate) are required for pea actin to retain DNase I binding ability. When adequate amounts of ATP are present, actin binding from the extract is further enhanced by basic pH, formamide, and soluble polyvinyl-pyrrolidone. Once actin is bound to the DNase I-agarose and washed free of extract, high ATP concentrations are not required to keep actin bound. Actin eluted from the DNase I-agarose with formamide retained its ability to polymerize into filaments with the addition of KCl and Mg(2+). The advantages and disadvantages of this procedure and its application to other plant materials are discussed.

Journal Article↗
PubMed1966

Sugars and Organic Acids of Vitis vinifera.

Glucose, fructose, galactose, sucrose, maltose, melibiose, raffinose, and stachyose were identified in the leaves, bark, roots, and berries of Vitis vinifera L. var. Thompson Seedless. In addition to these sugars, verbascose and manninotriose were found in the leaves and bark.Malic, tartaric, citric, isocitric, ascorbic, cis-aconitic, oxalic, glycolic, glyoxylic, succinic, lactic, glutaric, fumaric, pyrrolidone carboxylic, alpha-ketoglutaric, pyruvic, oxaloacetic, galacturonic, glucuronic, shikimic, quinic, chlorogenic, and caffeic acids were identified in the leaves, bark, roots, and berries.Glucose, fructose, sucrose, malate, tartrate, and citrate were determined quantitatively in the leaf, petiole, xylem, bark, tendril, bud, puduncle pedicel, berry, lateral roots, and main roots at 4 separate physiological stages of growth. In addition, changes in the concentrations of fructose, glucose, malate, and tartrate in leaves were measured during a 36-day period starting from budburst.

Journal Article↗
PubMed1974

The function of the carbohydrate units of three fungal enzymes in their resistance to dehydration.

Glucose oxidase (from Aspergillus niger), glucoamylase (from Rhizopus spp.), and cellulase (from Aspergillus niger) of fungal origin are all glycosylated proteins. Dehydration of the three enzymes to a range of water potentials did not affect their activity. However, when more than 10% of the carbohydrate associated with the molecules was removed by periodate oxidation, the enzymes were highly susceptible to dehydration when compared with oxidized controls. Polyvinyl pyrrolidone and Dextran T500 protected the three enzymes in their oxidized state against the effects of dehydration.The carbohydrate units of the enzymes have a function in protecting the enzymes from dehydration and this may be a contributing factor to the survival of microorganisms in environments of low water potentials. The involvement of water associated with the enzyme molecules due to the presence of carbohydrate units is considered to be the protecting mechanism.

Journal Article↗
PubMed1979

Purification and characterization of the carboxypeptidase isoinhibitors from potatoes.

Three zones of carboxypeptidase inhibitory activity were observed when heat-stable extracts of potato tubers (cv. Russet Burbank) were chromatographed on carboxymethyl cellulose. The isoinhibitors found in these zones were denoted I, II, and III based upon their order of elution from this column. The predominant form (II) had previously been suggested to be a mixture of two polypeptides (IIa and IIb) differing in that IIa possessed an additional residue of glutamine (Hass et al. 1975 Biochemistry 14: 1334). These closely related isoinhibitors (IIa and IIb) were separated by equilibrium ion exchange chromatography and characterized. Isoinhibitor I was shown to be identical to II except for two replacements, Ser-30 --> Ala and Arg-32 --> Gly. These replacements had no significant effect on apparent K(i) values toward either carboxypeptidase A or B. Isoinhibitor III, which was identical to II except that it lacked the amino terminal pyrrolidone carboxylic acid and following glutamine residue, was also functionally indistinguishable from II in inhibition studies. It was concluded that at least two and possibly as many as five genes code for the various isoinhibitor species which are present in potato tubers.

Journal Article↗
PubMed2000

Hydrophilic polymers derived from vitamin E.

Vitamin E containing copolymers for biomedical applications was obtained by copolymerization reaction of vitamin E methacrylate (VEMA) with 2-hydroxyethyl methacrylate (HEMA), N,N-dimethyl acrylamide (DMA) or vinyl pyrrolidone (VP), in different experiments. High molecular weight copolymers prepared by free radical reactions initiated by azobisisobutironitrilo, AIBN, present a random distribution of vitamin E derivatives along the macromolecular chains, and the average composition depends on the initial composition of the reaction medium. The relative flexibility of the polymeric systems was analyzed measuring the glass transition temperature of copolymeric sequences and that of the pure alternating diad (Tg12) obtained by the application of the treatments proposed by Johnston and Barton to all the systems. Tg12 was higher than the average T of both homopolymers (Tg) for the VEMA-HEMA system, Tg12 was lower than Tg for the VEMA-DMA system and Tg12 was similar to Tg for the VEMA-VP system. VEMA-HEMA copolymers gave rise to hydrogels in water, acidic and alkaline media. VEMA-DMA copolymers gave rise to hydrogels in acidic medium and dissolved in water and alkaline medium. VEMA-VP copolymers were soluble in all media. The swelling of all the hydrogels fit a second order kinetics. A VEMA-HEMA hydrogel was selected for in vivo experiments in order to study the influence of vitamin E on the regeneration process of Achilles tendon. The polymeric derivatives of vitamin E stimulated the regenerative process as a consequence of the antiaging effect in the local area of application.

Acrylamides↗
PubMed2002

A cyano-bridged dinuclear 4f-3d array.

A cyano-bridged bimetallic 4f-3d complex, triaqua-1 kappa(3)O-mu-cyano-1:2 kappa(2)N:C-pentacyano-2 kappa(5)C-tetrakis(2-pyrrolidone-1 kappa O)chromium(III)dysprosium(III) dihydrate, [CrDy(C(4)H(7)NO)(4)(CN)(6)(H(2)O)(3)] x 2H(2)O, has been prepared and characterized by X-ray crystallographic analysis. The structure consists of a neutral cyano-bridged Dy-Cr dimer. A hydrogen-bonded three-dimensional architecture is formed through N[bond]H...O, O[bond]H...N and O[bond]H...O hydrogen bonds.

Journal Article↗
PubMed1980

Studies on the accumulation of L-pyroglutamic acid in guinea pig epidermis.

The activities and properties of the enzymes involved in the formation and degradation of pyroglutamic acid (2-pyrrolidone-5-carboxylic acid, 5-oxoproline) in guinea pig epidermis have been studied. The enzyme pattern was characterized by an extremely high activity of gamma-glutamyl cyclotransferase. The epidermal extracts possessed a measurable, but rather low activity of pyroglutamate hydrolase. It is suggested that the only major pathway by which pyroglutamate may be formed in epidermal tissue is from L-glutamate by a 2-step reaction, the first involving the formation of a gamma-glutamyl peptide by the action of gamma-glutamyl-cysteine synthetase, and the second cyclization of the gamma-glutamyl moiety by the action of gamma-glutamyl cyclotransferase. Abundant substrate supply, the extremely high cyclotransferase activity and the rather low capacity to degrade pyroglutamate may be the factors responsible for the accumulation of this compound in epidermal tissue. A relatively low content of reduced glutathione may also be a contributing factor.

Animals↗
PubMed2006

Use of the dynamic vapor sorption meter to measure skin hydration properties, in vitro.

BACKGROUND: Maintaining an adequate skin moisture balance is important for retaining soft, pliable, healthy-looking skin. This report describes the use of the dynamic vapor sorption (DVS) meter to quantify water content of skin in vitro under a variety of conditions. It is the only instrument that couples an ultra-sensitive Cahn microbalance (resolution=0.1 microg) with an environmental system where both humidity and temperature are controlled. This feature is important since the skin's water content is influenced by changes in the relative humidity. METHOD: In every experiment, the temperature was held constant at 25 degrees C, and the starting relative humidity (RH) was set to 0% RH. The RH was programmed to step in 10% increments ending at 90% RH. The RH was incremented to the next level only when the mass change was less than 0.005%/min. RESULTS: A hysteresis was observed for all skin sorption/desorption experiments completed. Glycerin and the sodium salt of pyrrolidone carboxylic acid (NaPCA) both enhanced the % water content of skin. NaPCA was a more effective humectant at high relative humidities (above 60% RH); while glycerin performed better at humidities below 40% RH. Washing the skin with sodium lauryl sulfate (SLS) reduced the skin's ability to absorb water more so than washing with Tween 80, a milder surfactant. Vaseline petroleum jelly enhanced the water-retention properties of untreated skin. CONCLUSIONS: The DVS can effectively be used to study the sorption and desorption properties of skin. We have shown that the amount of water absorbed is influenced by the RH, the presence of humectants and/or occlusive agents, and surfactant harshness.

Absorption↗
PubMed2006

The use of near-infrared spectroscopy in skin care applications.

BACKGROUND: Near-infrared (NIR) spectroscopy was used to document the skin water content as a function of product usage and changes in the % relative humidity (%RH) in vitro and in vivo. The objective of the investigation was to determine if the NIR could provide comparable skin water content information as that obtained using gravimetric, conductivity, or visual assessment methods without having to invoke complex chemometric calculations. METHODS: NIR data were obtained using an NIR5000 spectrophotometer with a fiber optic probe (Smartprobe) attachment to complete the clinical studies and a Direct Contact Analyzer module to carry out the in vitro experiments. Conductivity measurements were completed using the Skicon 200, which measures conductance at a fixed frequency of 3.5 MHz. Three moisturization-based clinical studies were carried out assessing the NIR's ability to detect skin hydration changes. In Clinical Study A, NIR and Skicon data were collected for panelists who had only washed their outer calf with water over a 4-week period. During this time, the daily average %RH was recorded. In Clinical Study B, 10% solutions of glycerin, choline chloride, and the sodium salt of pyrrolidone carboxylic acid were applied to the panelist's outer calf and biophysical measurements were completed to assess the hydration and desorption properties of these humectants. In Clinical Study C, a 10% solution of choline chloride was applied to panelist's outer calf and the cumulative effect of using this product was evaluated over a 3-week period. For all in vitro studies, porcine skin was used as the substrate. RESULTS: Comparable NIR, Skicon, and visual dryness results were obtained for most of the product usage-based clinical experiments completed. However, the NIR was particularly more effective at detecting skin water content differences as a function of %RH changes. In the absence of abrupt (>50%) relative humidity variations, there was a direct correlation between the NIR readings and the %RH (R(2)=0.83) unlike what was observed for the Skicon measurements (R(2)=0.22). CONCLUSIONS: NIR spectroscopy demonstrated the changes in the skin water content as a function of product usage; the results were consistent with those obtained using the Skicon conductivity meter and visual dryness assessment scores. More importantly, the differences detected were obtained without having to use chemometric manipulations in the data analysis as is the common practice. Of all the methods used, the NIR gave the best linear regression for %RH-induced skin water content changes.

Animals↗
PubMed1994

Differential effect of duocarmycin A and its novel derivative DU-86 on DNA strand breaks in HeLa S3 cells.

Duocarmycin A (DUMA) and DU-86, a semisynthetic derivative of duocarmycins (DUMs) and a possible active form of KW-2189, both showed potent cell growth-inhibitory and cell-killing activities against human uterine cervix carcinoma HeLa S3 cells. Both drugs showed similar profiles of inhibition of macromolecular synthesis and influence on cell-cycle distribution. Namely, they inhibited [3H]thymidine uptake at lower concentrations than [3H]uridine or [3H]leucine uptake, suggesting that the inhibition of DNA synthesis is the primary site of their actions. Furthermore, they induced the accumulation of cells in early S phase. However, a significant difference was observed between these drugs in terms of DNA-fragmentation activity against HeLa S3 cells by using two independent methods, pulse-field gel electrophoresis and alkaline elution. DNA fragmentation was insignificant in the cells treated with DU-86, in contrast to the cells treated with DUMA. The analysis of DNA adducts in the cells revealed that DU-86 alkylated adenine quite selectively, while DUMA alkylated both adenine and guanine. These results suggest that the pyrrolidone ring of DUMA is responsible for its adduct formation with guanine and the subsequent DNA-fragmentation and inhibition of DNA synthesis, while DU-86 alkylated adenine and inhibited DNA synthesis through mechanisms other than DNA-fragmentation.

Adenine↗
PubMed1979

Synthesis of a series of residue 1 (pyroglutamic acid) analogs of thyrotrophin releasing hormone.

This report describes the synthesis of 23 analogs of thyrotrophin releasing hormone, L-pyroglutamic acid-L-histidyl-L-prolineamide, where only the pyroglutamic acid moiety is modified. Twelve of the analogs contain different heterocyclic rings or are derivatized pyrrolidone rings. The syntheses of these pyroglutamic acid analogs are also described. Peptide bond formation was generally achieved by catalyzing carbodiimide coupling with 1-hydroxybenzotriazole. The histidine side chain was protected with the 2,4-dinitrophenyl group during di- and tripeptide synthesis and was removed with benzenethiol Final purification of tripeptides involved passage of synthetic material over a Dowex 1--X4 (bicarbonate) column. The route for synthesis of thyrotrophin releasing hormone and its analogs is highly efficient, since the native hormone may be obtained with 90% efficiency.

Amino Acids↗
PubMed1981

Partial molar heat capacity of the peptide group in aqueous solutions.

Integral enthalpies of solution at very high dilution of sodium salts of N-acetyl amino acids, N-acetyl peptides, and N-benzoyl glycine have been measured in water at 298.15 and 308.15 K. Standard heat capacities of solution at 303.15 K have been derived from the enthalpy of solution data. The peptide backbone-unit (CH2CONH) contribution toward the limiting partial molal heat capacities derived from these experimental results is compared with those obtained from Cop2 of other model compounds, viz. oligopeptides, pyrrolidones, piperidones, diketopiperazine, and amides. Cop2 of the peptide backbone unit observed in the sodium slats of the N-substituted amino acids and peptides is also correlated with the structural details of the compounds and it is concluded that Cop2 contribution of the whole CH2CONH group, rather than that of CONH group, should be used for predicting the heat capacities of polypeptides and proteins in aqueous solution.

Calorimetry↗
PubMed2005

Facile solid-phase synthesis of C-terminal peptide aldehydes and hydroxamates from a common Backbone Amide-Linked (BAL) intermediate.

C-Terminal peptide aldehydes and hydroxamates comprise two separate classes of effective inhibitors of a number of serine, aspartate, cysteine, and metalloproteases. Presented here is a method for preparation of both classes of peptide derivatives from the same resin-bound Weinreb amide precursor. Thus, 5-[(2 or 4)-formyl-3,5-dimethoxyphenoxy]butyramido-polyethylene glycol-polystyrene (BAL-PEG-PS) was treated with methoxylamine hydrochloride in the presence of sodium cyanoborohydride to provide a resin-bound methoxylamine, which was efficiently acylated by different Fmoc-amino acids upon bromo-tris-pyrrolidone-phosphonium hexafluorophosphate (PyBrOP) activation. Solid-phase chain elongation gave backbone amide-linked (BAL) peptide Weinreb amides, which were cleaved either by trifluoroacetic acid (TFA) in the presence of scavengers to provide the corresponding peptide hydroxamates, or by lithium aluminum hydride in tetrahydrofuran (THF) to provide the corresponding C-terminal peptide aldehydes. With several model sequences, peptide hydroxamates were obtained in crude yields of 68-83% and initial purities of at least 85%, whereas peptide aldehydes were obtained in crude yields of 16-53% and initial purities in the range of 30-40%. Under the LiAlH4 cleavage conditions used, those model peptides containing t-Bu-protected aspartate residues underwent partial side chain reduction to the corresponding homoserine-containing peptides. Similar results were obtained when working with high-load aminomethyl-polystyrene, suggesting that this chemistry will be generally applicable to a range of supporting materials.

Aldehydes↗
PubMed1975

Anticomplementary activity of human immunoglobulin G. I. Mechanism of the artifactual increase in anticomplementary activity of IgG during the assay.

The anticomplementary activity of IgG can be increased up to 20-fold by pipetting during the preparation of serial dilutions for the assay of this activity. Albumin, if added to the IgG solution before the serial dilutions, completely prevents this artifactual increase in activity. Polyethylene glycol, polyvinyl pyrrolidone, methyl cellulose, gelatin and octanol are also effective stabilizers of IgG. Repeated pipetting of IgG solutions caused marked linear increase in their anticomplementary activity. The formed anticomplementary activity was due to small amounts of highly aggregated protein. The amount of activity formed depended on at least four factors: [1] the number of pipetting steps; [2] the IgG concentration; [3] the level of albumin or other stabilizers, and [4] the pH, which influences the stabilization by albumin. The anticomplementary activity of IgG is increased up to 100-fold by exposure to gas-liquid, liquid-liquid and hydrophobic solid-liquid interfaces. Albumin and polyethylene glycol prevent the activity increase during these treatments. The tendency of IgG to aggregate at interfaces and the ability of albumin and other substances to prevent the aggregation paralleled their rate of adsorption to the air-water interface. Solutions of dansyl chloride in decane emulsified in aqueous solutions of IgG and albumin specifically label the proteins at the liquid-liquid interfaces. The mechanism of stabilization can be explained by preferential adsorption of surface-active proteins and polymers.

Chemical Precipitation↗
PubMed1985

Quantitative differential agglutination method using the Coulter Counter to measure survival of compatible but identifiable red blood cells.

The method described here using a centrifuge and Coulter Cell Counter for the quantitative differential agglutination of human red cells uses commercial anti-A and anti-B antisera for the ABO system, and for the Rh system a commercial anti-D serum, a low ionic strength solution and an anti-human IgG antiserum. We compared this Coulter Counter method with the Technicon AutoAnalyzer method which utilizes bromelin and polyvinyl pyrrolidone, and anti-A, anti-B and anti-CD antisera, and found this new method to be the simpler of the two. The nonagglutinable count with the Coulter Counter was 1.07% for A1 red cells, 2.26% for A2 red cells, 1.06% for B red cells, and 1.78% for Rh-positive red cells, results similar to those seen with the Technicon AutoAnalyzer. Results with the Coulter Counter method were consistently accurate whether the ACD red cells were studied on the day of collection, after 10 days of 4 degrees C storage, or after 4 degrees C storage for up to 6 days followed by cryopreservation with 40% (w/v) glycerol at-80 degrees C, thawing and washing. In this study, red cell samples obtained from recipients who had received compatible but identifiable donor red cells were frozen with 40% glycerol and stored at-80 degrees C for 10 months, thawed and washed. Survival measurements on these washed previously frozen red cells were similar to the values in liquid-stored red cells.

Agglutination Tests↗
PubMed1980

The primary structure of amyloid fibril protein AA in endotoxin-induced amyloidosis of the mink.

Two AA proteins were isolated from the same amyloid fibril preparation from the liver of a mink, in which amyloidosis had been induced by injections with endotoxin. The two proteins were of different size, one containing 53 amino acid residues and the other 64 residues. The amino acid sequence was otherwise found to be identical. Both proteins revealed pyrrolidone carboxylic acid as the N-terminal amino acid. Sequence homologies with protein AA from other species were very striking. However, no antigenic cross-reaction was seen between mink protein AA and antisera to protein AA from human, mouse or rabbit sources.

Amino Acid Sequence↗