Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Transition Temperature”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

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

At least 469 records · Page 26Linked to original sources
PubMed1985

Modulation of (Na+,K+)-ATPase activity by the lipid bilayer examined with dansylated phosphatidylserine.

The fluorescent probe 8-(dimethylamino)naphthalene-1-sulfonylphosphatidylserine (Dns-PS) was incorporated into purified lamb kidney Na+- and K+-stimulated adenosinetriphosphatase (EC 3.6.1.3) [(Na+,K+)-ATPase] by using a purified phospholipid exchange protein. Phospholipase C was used to reduce phospholipid content. Up to 40% of the phospholipid could be hydrolyzed with only 10% inhibition of the (Na+,K+)-ATPase, but when 67% of the phospholipid was hydrolyzed, the enzyme was inhibited 53%. To examine the effect of protein on the phospholipid bilayer, the fluorescent parameters of the probe incorporated into the enzyme preparation were contrasted with the same parameters for the probe incorporated into the total lipid extract of the preparation. The polarization of fluorescence of the probe in the lipid extract was 0.118 while in the enzyme preparation it was 0.218. This reflected a decrease in fluidity of the glycerol region of the phospholipid bilayer which was mediated by the protein. This effect increased as the phospholipid content of the (Na+,K+)-ATPase preparation was reduced so that with maximal phospholipid reduction the polarization of fluorescence was 0.262. The protein caused a decrease in the transition temperature from gel to fluid states of the bilayer detected by polarization of the probe. The midpoint temperature transition of the enzyme preparation decreased from 33 degrees C when all phospholipids were present to 20 degrees C when 67% of the phospholipids were hydrolyzed. This decrease was not observed for the lipid extract of these samples. A direct correlation between the (Na+,K+)-ATPase specific activity and the polarization of fluorescence of Dns-PS was found. The reduction in phospholipid content did not affect the steady-state level of phosphorylation of the enzyme by ATP but did affect the rate of dephosphorylation which would require conformational changes of the enzymes. The data showed that the fluidity of the phospholipid bilayer can modulate the activity of the (Na+,K+)-ATPase.

Animals↗
PubMed1976

Effect of lipids on the reconstitution of D-lactate oxidase in Escherichia coli membrane vesicles.

An unsaturated fatty acid auxotroph lacking D-lactate dehydrogenase activity has been isolated from Escherichia coli ML 308-225 dld-3. While NADH oxidase activity in membrane vesicles prepared from the mutant cells grown in a variety of unsaturated fatty acids is comparable to that of previously isolated fatty acid auxotrophs, D-lactate oxidase activity is absent. However, D-lactate oxidase ativity can be restored when vesicles are incubated with a purified preparation of D-lactate dehydrogenase obtained from wild type cells. The effect of altering the fatty acid composition of the membrane on the reconstitution of D-lactate oxidase activity was examined. Binding of purified D-lactate dehydrogenase was not affected by either the lipid composition of the membrane vesicles or the temperature during reconstitution. However, the reconstitution of D-lactate oxidase activity was strongly influenced by the fatty acid composition of the membrane lipids. The temperature dependence of the reconstituted activity was analyzed. Temperature transitions were not observed with membrane vesicles supplemented with oleic or linolenic acid but palmitelaidic acid-enriched vesicles exhibited a transition temperature at 30 degrees. Attempts to reconstitute the elaidic-supplemented vesicles at temperatures below 30 degrees failed to yield active D-lactate oxidase and the vesicles aggregated. At 42 degrees, aggregation did not occur and D-lactate oxidase activity was obtained to a level of 10% of that found with membranes from the parent strain (ML 308-225). These results suggest that although binding of D-lactate dehydrogenase is independent of the physical state of the membrane, reconstitution of the D-lactate oxidase activity in membrane vesicles is dependent upon the fatty acid composition of the phospholipid, hence the physical state of the membrane.

Cell Membrane↗
PubMed1985

In vitro characterization of hybrid promoters and altered tryptophan operon promoters.

This study examines the in vitro interaction of hybrid and altered Escherichia coli promoters and other promoters with purified E. coli RNA polymerase. Three parameters of polymerase activity were examined: the time for open complex formation; the temperature of transitions; and the time required for productive initiation. The results indicate the rate of in vitro binding as measured by the filter binding technique does not completely correlate with the in vivo activities among these diverse promoters. Transition temperatures ranged from 13 to 27 degrees C with the lowest transition temperatures associated with the relatively weak in vivo beta-lactamase and anti-tet promoters. The productive initiation studies showed a dependence on labeled nucleoside triphosphate concentration when that nucleotide was present early and frequently in the transcript. Promoters containing the -10 region of the lac promoter had slow productive initiation rates while trp -10 promoter derivatives were generally very fast. In the promoters studied here, a trend was noted between the binding rate and transition temperature studies in that the promoters with the lower transition temperatures tended to bind more rapidly.

Cytidine Triphosphate↗
PubMed1997

Differential scanning calorimetry and CD spectrometry of acclimation temperature-associated types of carp light meromyosin.

Differential scanning calorimetry and CD spectrometry were employed to study the thermal unfolding of light meromyosin (LMM) prepared from carp acclimated to different temperatures. The transition temperatures given by the major peaks at pH 8.0 in 0.6 M KCl for LMM from carp acclimated to 10 degrees C were 32.5 and 39.5 degrees C with the calorimetric enthalpies (DeltaHcal) of 269 and 52 kcal/mol, respectively. LMM from carp acclimated to 20 degrees C exhibited three peaks of transition temperatures at 34.5, 40.2, and 46.9 with DeltaHcal of 152, 20, and 10 kcal/mol, respectively. On the other hand, LMM from carp acclimated to 30 degrees C showed two different patterns. The first experiment gave two transition temperatures at 39.2 and 47.3 degrees C with DeltaHcal of 231 and 39 kcal/mol, respectively. The second series of experiments resulted in showing three peaks of 34.4, 39.5, and 47.5 degrees C with DeltaHcal of 117, 123, and 28 kcal/mol, respectively. N-terminal amino acid sequence analysis revealed that LMM at the second series of experiments with the 30 degrees C-acclimated carp contained component(s) predominant in the 20 degrees C-acclimated carp. Thermal unfolding responsible for these transition temperatures was well explained by melting of alpha-helices which could be determined by far-ultraviolet CD spectroscopy. These results clearly demonstrate that the 30 degrees C-acclimated carp contained the most thermostable LMM.

Acclimatization↗
PubMed1989

Monoclonal antibodies as probes for monitoring the denaturation process of bovine beta-lactoglobulin.

Five monoclonal antibodies (MAbs) of different idiotypes were produced against bovine beta-lactoglobulin (beta-LG). Among them, MAbs 61B4 and 62A6 reacted preferentially to native beta-LG, while MAbs 21B3 and 31A4 reacted more strongly to the reduced carboxymethylated (denatured) beta-LG than to the native material. These two types of MAb were used to analyze the denaturation process of a beta-LG molecule during heating. The binding affinity of MAbs 21B3 and 31A4 with beta-LG was increased by increasing the heating temperature, the transition temperature being 67-68 degrees C, while that of MAbs 61B4 and 62A6 was reduced by increasing the temperature, this transition temperature being about 80 degrees C. Epitopes recognized by MAbs 31A4 and 61B4 were shown to be included in the segments, Lys8-Trp19 (mostly in the random-coil region) and Thr125-Lys135 (helical region), respectively. The heat-induced conformational change of the beta-LG molecule is, therefore, likely to start in random-coil region as Lys8-Trp19, and to be followed by a structural change in a helical region as Thr125-Lys135. This study demonstrates that MAb is a useful probe to monitor local conformational changes of a protein molecule during denaturation.

Animals↗
PubMed1994

[The effects of environmental thermal condition on transitional skin temperature of peripheral parts of human hands and feet during exercise].

The effects of environmental temperature on transitional skin temperatures of peripheral parts of human hands and feet were examined during exercise to obtain basic information on thermal characteristics of heat transfer from human body to the environment. Very thin and fat male adults served as subjects who were in contrast regarding fat content. Their skin temperatures were undertaken by thermocouples in a climate chamber. The exercise was made using an ergometer at three stages of the chamber temperatures. The skin temperature of a fat subject's trunk was observed to be lower than that of thin subject due to the insulation of fat in the body. In compensation for less heat transfer from the trunk, the temperatures of peripheral parts of fat subject's hands and feet were higher than that of the thin subject. Moreover, the response of the temperature to the thermal load due to exercise was observed to be quicker. These kinds of variation were considered as due to the increase in blood flow through arteriovenous anastomoses, AVA. It seemed that AVA blood of the thin subject did not increase during resting condition at the environmental temperatures of 10 and 20 degrees C but was accelerated by the thermal load due to exercise. In addition, the response of AVA on the foot seemed to be delayed compared with that on the hand.

Adult↗
PubMed2003

Temperature-induced valence transition and associated lattice collapse in samarium fulleride.

The different degrees of freedom of a given system are usually independent of each other but can in some materials be strongly coupled, giving rise to phase equilibria sensitively susceptible to external perturbations. Such systems often exhibit unusual physical properties that are difficult to treat theoretically, as exemplified by strongly correlated electron systems such as intermediate-valence rare-earth heavy fermions and Kondo insulators, colossal magnetoresistive manganites and high-transition temperature (high-T(c)) copper oxide superconductors. Metal fulleride salts-metal intercalation compounds of C60--and materials based on rare-earth metals also exhibit strong electronic correlations. Rare-earth fullerides thus constitute a particularly intriguing system--they contain highly correlated cation (rare-earth) and anion (C60) sublattices. Here we show, using high-resolution synchrotron X-ray diffraction and magnetic susceptibility measurements, that cooling the rare-earth fulleride Sm2.75C60 induces an isosymmetric phase transition near 32 K, accompanied by a dramatic isotropic volume increase and a samarium valence transition from (2 + epsilon) + to nearly 2 +. The negative thermal expansion--heating from 4.2 to 32 K leads to contraction rather than expansion--occurs at a rate about 40 times larger than in ternary metal oxides typically exhibiting such behaviour. We attribute the large negative thermal expansion, unprecedented in fullerene or other molecular systems, to a quasi-continuous valence transition from Sm(2+) towards the smaller Sm((2+epsilon)+), analogous to the valence or configuration transitions encountered in intermediate-valence Kondo insulators like SmS (ref. 3).

Journal Article↗
PubMed1991

Low levels of the pesticide, delta-hexachlorocyclohexane, lyses human erythrocytes and alters the organization of membrane lipids and proteins as revealed by Raman spectroscopy.

We studied the nature of the interaction of delta-hexachlorocyclohexane (delta-HCCH), a pesticide having a stereoisomeric structure similar to inositol, with red blood cells. Cell survival data, measured as percent of hemoglobin released by delta-HCCH, show that the cell lysis increases with post exposure time. delta-HCCH at 55-60 micrograms/ml causes about 70% cell lysis after 24 h of exposure. The nature of interaction of delta-HCCH with membrane components was evaluated by studying the thermotropic transitions and protein structure of ghosts using Raman spectroscopy. Control ghosts show transitions with onset/completion temperatures 30 degrees C/38 degrees C (high temperature transition) and 3 degrees C/10 degrees C (middle temperature transition) when monitored by the I2935/I2850 ratio. The interaction of delta-HCCH drastically broadens the high temperature transition and shifts it to the temperature range of 10-29 degrees C. The plots of (I2880-90/I2850) vs. temperature show two transitions for control ghosts, one extending from -10 degrees C to 3 degrees C (lower temperature transition) and the other from about 7 degrees C to about 15 degrees C (middle temperature transition). Ghosts lysed with delta-HCCH shows only a single and a very broad transition in the range of about -3 degrees C to about 15 degrees C. These changes in the thermal transition properties suggest that delta-HCCH alters lipid and lipid-protein phases of erythrocyte membranes. The comparison of Raman spectra in the amide I and III regions of erythrocyte ghosts and purified band 3 with several amidated compounds reveals that cytoskeleton proteins contain highly amidated residues (probably glutamine and asparagine). The interaction of delta-HCCH with erythrocytes drastically alters the environment of these amidated residues indicating the involvement of cytoskeleton proteins. We conclude that the interaction of delta-HCCH with red blood cells disrupt membrane structure and change the environment of cytoskeleton proteins that could cause cell lysis.

Amides↗
PubMed1987

Compositional and Thermal Properties of Thylakoid Polar Lipids of Nerium oleander L. in Relation to Chilling Sensitivity.

The polar lipid classes from thylakoids of Nerium oleander L. were studied with the aim of relating changes in their composition and thermal behavior with reported changes in the transition temperature of their polar lipids and chilling sensitivity of their leaves. With an increase in growth temperature, the transition temperature of phosphatidylglycerol increased from 16 degrees C to 26 degrees C, and for sulfoquinovosyldiacylglycerol from 19 degrees C to 24 degrees C. Transitions in the other lipid classes were below -10 degrees C for plants grown at both growth temperature. The major changes in the molecular species of phosphatidylglycerol, with increasing growth temperature, were an increase in 1-oleoyl-2-palmitoyl phosphatidylglycerol from 21 to 39% and a decrease in 1-oleoyl-2-trans-3-hexadecanoic phosphatidylglycerol from 51 to 25%. Although the disaturated species increased from 8 to 23%, the maximum was less than that reported for chilling-sensitive plants. There was no change in the sum of the palmitic, hexadeca-trans-3-enoic and stearic acids. Dipalmitoyl sulfoquinovosyldiacylglycerol increased from 12 to 20% and 1-linolenoyl-2-palmitoyl sulfoquinovosyldiacylglycerol decreased from 40 to 30%. It is concluded that the increase in the transition temperature of the polar lipids and the sensitivity of acclimated oleander plants to chilling could not be predicted by the absolute sum of the saturated fatty acids or disaturated molecular species in phosphatidylglycerol. The polar lipid transition appears to be a product of mixing of both high and low melting-point lipids.

Journal Article↗
PubMed1977

Temperature induced transition of the pH-activity curve of heavy meromyosin adenosine triphosphatase and inosine triphosphatase.

The pH-activity curve of heavy meromyosin ATPase [EC 3.6.1.3] was measured at various temperatures. The pH-activity curve at higher temperatures showed a maximum at low pH and a minimum at pH 7 to 8 as has been already reported. At lower temperatures it was sigmoidal in shape, similar to a simple dissociation curve of pKa 6 to 7. The pH-activity curve at intermediate temperatures appeared to be inbetween the two extreme shapes. These changes in pH-activity curve with temperature were found to be common in the presence of divalent cations such as Mg2+, Mn2+, and Ca2+. The ATPase mechanism may be identical in the presence of any divalent cation, and the rate determining step revealing the steady state rate alters by changing the temperature. The transition temperatures estimated at pH 8 were 10 degrees, 8 degrees, and about 5 degrees in the presence of MnCl2, CaCl2, and MgCl2, respectively. The difference in the temperature coefficients above and below the transition temperature was most distinct in the presence of MnCl2, and vague in the presence of CaCl2. A similar change of pH-activity curve with temperature was found with heavy meromyosin ITPase in the presence of MgCl2.

Adenosine Triphosphatases↗
PubMed2002

Reconsideration of drug release from temperature-sensitive liposomes.

The liposomal phase transition temperature was monitored in unstirred suspensions using a differential scanning calorimeter. The main and pre-transition temperatures under conditions of stirring were measured by the change in 90 degrees light scattering using a fluorescence spectrophotometer. Both methods show the same main transition temperature either with or without stirring. Temperature sensitive liposomes were made of DPPC (dipalmitoylphosphatidylcholine), DMPC (dimylisitoylphosphatidylcholine) or DSPC (distearoylphosphatidylcholine). The calcein release profile from the liposomes depends on the stirring time of the liposome suspension at the main transition temperature. For 1 h incubation, the leakage profile with and without stirring is similar. It had been hypothesized that temperature sensitive liposomes released drug at the main-transition temperature. However, calcein leakage from liposomes is observed also at the pre-transition temperature. Thus, a liposomal encapsulated drug will likely leak from DPPC liposomes at body temperature (37 degrees C), even if the liposomes were designed to have a higher main transition temperature.

Calorimetry, Differential Scanning↗
PubMed2005

Spin glasses in the limit of an infinite number of spin components.

We consider spin glass models in which the number of spin components m is infinite. In the formulation of the problem appropriate for numerical calculations proposed by several authors, we show that the order parameter defined by the long-distance limit of the correlation functions is actually zero and there is only "quasi-long-range order" below the transition temperature. Nonetheless, there can be a finite temperature phase transition where the decay of correlations changes from exponential to power law. We also show that the spin glass transition temperature is zero in three dimensions so power-law behavior only occurs at T=0 in this case. We also argue that the order of limits, m-->infinity and N-->infinity is important, where N is the number of spins.

Journal Article↗
PubMed2003

Effect of sodium tetraborate (borax) on the thermal properties of frozen aqueous sugar and polyol solutions.

The effect of sodium tetraborate (Na(2)B(4)O(7), borax) on the thermal property of frozen aqueous sugar and polyol solutions was studied through thermal analysis. Addition of borax raised the thermal transition temperature (glass transition temperature of maximally freeze-concentrated solutes; T(g)') of frozen sucrose solutions depending on the borax/sucrose concentration ratios. Changes in the T(g)' of frozen mono- and disaccharide solutions suggested various forms of complexes, including those of a borate ion and two saccharide molecules. Borax exerted the maximum effect to raise the oligosaccharide and dextran T(g)'s at borax/saccharide molar ratios of approximately 1-2 (maltose and maltooligosaccharides), 2 (dextran 1060), 5 (dextran 4900), and 10 (dextran 10200). Further addition of borax lowered T(g)'s of the saccharide solutions. Borax also raised T(g) and T(g)' temperatures of frozen aqueous glycerol solutions. The decreased solute mobility in frozen solutions by the borate-polyol complexes suggested higher collapse temperature in the freeze-drying process and improved stability of biological systems in frozen solutions.

Borates↗
PubMed2004

Effects of sodium tetraborate and boric acid on nonisothermal mannitol crystallization in frozen solutions and freeze-dried solids.

The purpose of the present study was to elucidate the effects of sodium tetraborate (borax) and boric acid on the crystallization of mannitol in frozen aqueous solutions and freeze-dried solids. Thermal analysis of frozen solutions showed that sodium tetraborate inhibits mannitol crystallization at sodium tetraborate/mannitol molar concentration ratios of approximately 0.05, which is much lower than the other co-solutes studied (boric acid, sucrose, sodium phosphate buffer). Inhibition of the mannitol crystallization in frozen solutions resulted in highly amorphous mannitol in the freeze-dried solids. Mannitol remained in an amorphous state in some of the combination freeze-dried solids, even at elevated temperatures. Changes in the thermal transition temperatures (glass transition temperature of maximally freeze-concentrated solute ( T'g) and glass transition temperature of freeze-dried solid (Tg)) suggested reduced mannitol molecular mobility with increases in the sodium tetraborate ratio. Fourier-transform infrared spectroscopy (FT-IR) analysis of the bovine serum albumin secondary structure showed apparent protein structure-stabilizing effects of the amorphous mannitol and sodium tetraborate combination during the freeze-drying process. The mannitol and sodium tetraborate combination also protected lactate dehydrogenase (LDH) from inactivation during freeze-drying. We conclude that the complex formation and the accompanying reduction in molecular mobility make sodium tetraborate an effective mannitol crystallization inhibitor in frozen solutions and freeze-dried solids.

Animals↗
PubMed1975

The effect of chain length and lipid phase transitions on the selective permeability properties of liposomes.

This paper describes experiments showing the importance of the fatty acid chain length on the barrier properties of liposomal bilayers, prepared from saturated lecithins, under conditions of lateral phase separation. 1. Above the gel to liquid crystalline phase transition temperature, liposomes prepared from saturated lecithins with 14 or more carbon atoms per acyl chain exist as stable bilayers, which are practically impermeable to ions. 2. At temperatures well above the transition temperature dilauroyl phosphatidylcholine liposomes exhibited osmotic shrinkage, which was dependent on the ionic size of the solute used to bring about the osmotic gradient, indicating that the permeation through these less stable bilayers takes place mainly via individual diffusion of the permeating ions. 3. An enhanced release of trapped potassium from liposomes was demonstrated in the vicinity of the transition temperature. The extent of the increase, however, depended strongly on the length of the paraffin chain. 4. From measurements of the shrinkage behaviour of liposomes in the vicinity of the transition temperature it is concluded that the increased permeability decreases with increasing diameter of the permeating ion. This finding implies that the increased permeability at the transition temperature cannot be ascribed to "macroscopic" rupture of the liposomal membrane. The maximum permeability in the vicinity of the Tc is discussed in terms of probability and size distribution of statistical pore formation at the boundaries of liquid and solid domains.

Cations, Monovalent↗
PubMed1982

Phospholipid-nucleoside conjugates. The aggregational characteristics and morphological aspects of selected 1-beta-D-arabinofuranosylcytosine 5'-diphosphate-L-1,2-diacylglycerols.

1-beta-D-Arabinofuranosylcytosine 5'-diphosphate-1,2-diacylglycerols have previously been shown to be promising candidates as prodrugs of the clinically useful antileukemic agent 1-beta-D-arabinofuranosylcytosine. Because of the amphipathic nature of these liponucleotides and the potential that their morphological state may mediate their biological activity, it was necessary to undertake detailed studies of their aggregational and morphological characteristics. When samples of 1-beta-D-arabinofuranosylcytosine 5'-diphosphate-L-1,2-diacylglycerols (containing either dimyristoyl, dipalmitoyl or distearoyl fatty acid side chains) were prepared in buffered saline solutions using sonication methods, the morphological nature of the resulting aggregate was shown to be related to temperature and the length of the side chain. When sonicated at low temperatures all the above-mentioned derivatives gave turbid solutions containing large bilayer sheets. As the temperature was raised, a transition temperature was reached at which a stable three-dimensional cross-linked network of small interlocking bilayer stacks was formed. This turbidity transition temperature was directly related to the chain length of the fatty acid side chain. Sonication at temperatures close to this turbidity transition temperature produced small disc-shaped micellar structures. These micelles were shown to exist in another aggregational equilibrium consisting of a stacking-destacking process, the position within this equilibrium being dependent upon the concentration. In contrast, a sample of 1-beta-D-arabinofuranosylcytosine 5'-diphosphate-L-1,2-dioleoylglycerol (which contains an unsaturated carbon-carbon bond in each of the fatty acid side chains) was shown to give a multilamellar liposome structure when sonicated in buffered saline at temperatures above its turbidity transition temperature.

Antineoplastic Agents↗
PubMed2000

Quantum-critical conductivity scaling for a metal-insulator transition

Temperature (T)- and frequency (omega)-dependent conductivity measurements are reported here in amorphous niobium-silicon alloys with compositions (x) near the zero-temperature metal-insulator transition. There is a one-to-one correspondence between the frequency- and temperature-dependent conductivity on both sides of the critical concentration, thus establishing the quantum-critical nature of the transition. The analysis of the conductivity leads to a universal scaling function and establishes the critical exponents. This scaling can be described by an x-, T-, and omega-dependent characteristic length, the form of which is derived by experiment.

Journal Article↗