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PubMed1995

Effect of separation conditions on automated isoelectric focusing of carbohydrate-deficient transferrin and other human isotransferrins using the PhastSystem.

To investigate the effect of automated isoelectric focusing conditions in the PhastSystem, e.g., the point of sample application, prerun and separation times, and minimized gels on isotransferrin band pattern, human sera were analyzed with native transferrin iron load, after iron saturation or iron depletion in vitro. Varying the focusing conditions we found (i) Point of sample application (anode, middle of the gel, cathode) strongly affected transferrin iron loss. It was greatest at the anode and least at the cathode. (ii) Without prerun, distinct transferrin iron loss also occurred. A short prerun time prevented iron loss, but increasing it did not improve transferrin iron load stability as stated by others. (iii) An inappropriately long separation time inevitably yielded iron loss. In conclusion, inappropriate isoelectric focusing conditions strongly affect iron load stability of isotransferrins (obviously via low pH within the gel), resulting in transferrin iron release and cofocusing of isotransferrins with different sialic acid or iron contents. For determination of carbohydrate-deficient transferrin, such conditions resulted in overestimation of the marker of chronic alcohol abuse. Our findings may be of guiding importance for isoelectric focusing of protein-ligand complexes. We recommend the procedure described for development of isoelectric focusing of protein-ligand complexes.

Carbohydrates↗
PubMed2002

The improvement of lipase secretion and stability by addition of inert compounds into Acinetobacter calcoaceticus cultures.

Acinetobacter calcoaceticus BD413 produces variable amounts of an exocellular lipase that becomes rapidly inactivated upon secretion. To achieve high yield and protect the enzyme, we assayed the addition of several inert compounds to cell-free supernatants, cell fractions, and whole cultures. Glass beads, poly(ethylene glycol) 600, Triton X-100, saccharose, gum arabic, and beta-cyclodextrin were among the compounds tested. beta-Cyclodextrin and gum arabic (and saccharose to a lesser extent) were effective enzyme stabilizers in cell-free supernatants, while gum arabic, glass beads, and Triton X-100 improved lipase secretion from cells, and, therefore, total lipase yield (30-50%, according to the additive). In whole cultures, beta-cyclodextrin was the most effective additive, particularly in combination with glass beads or gum arabic. Indeed, cultures containing beta-cyclodextrin plus gum arabic were able to maintain 95% (+/- 1.5%) of the initial lipase activity for more than 16 h, while control cultures with no additives maintained only 10% (+/- 4%) of the enzyme activity after the same period. In conclusion, the addition of inert compounds in cultures may be considered a useful approach for achieving increased yield and lipase stabilization, amenable for downstream processing.

Acinetobacter calcoaceticus↗
PubMed1985

Analysis of the factors and implications of an empirical method for estimating the stability of mutant human haemoglobins.

An empirical method for estimating the effects of single amino acid substitutions on structural stability of proteins with known spatial structure is developed. Twenty physical and chemical properties of amino acids and characteristics of protein tertiary structure were analysed to determine those most involved in producing instability. We employed data on 330 mutant variants of the alpha- and beta-subunits of human haemoglobin in choice of the parameters of the method developed which yielded a 81% of prediction accuracy of stability estimates for human mutant haemoglobins.

Amino Acid Sequence↗
PubMed2005

Gel trapping of dense colloids.

Phase density differences in sols, foams, or emulsions often lead to sedimentation or creaming, causing problems for materials where spatial uniformity over extended periods of time is essential. The problem may be addressed through the use of rheology modifiers in the continuous phase. Weak polymer gels have found use for this purpose in the food industry where they appear to be capable of trapping dispersoid particles in a three-dimensional matrix while displaying water-like viscosities at low shear. Attempts to predict sedimentation stability in terms of particle properties (size, shape, density difference) and gel yield stress have led to qualitative success for suspensions of large particles. The effect of particle size, however, in particular the case in which colloidal dimensions are approached, has not been investigated. The present work seeks to determine useful stability criteria for colloidal dispersions in terms of readily accessible viscoelastic descriptors. Results are reported for systems consisting of 12 microm poly(methyl methacrylate) (PMMA) spheres dispersed in aqueous gellan gum. Monovalent salt concentration is varied to control rheological properties, and sedimentation/centrifugation experiments are performed to determine dispersion stability. Necessary conditions for stability consist of a minimum yield stress together with a value of tan delta less than unity.

Journal Article↗
PubMed2001

The floating shoulder: a biomechanical basis for classification and management.

BACKGROUND: The floating shoulder (ipsilateral fractures of the clavicular shaft and the scapular neck) is thought to be an unstable injury pattern requiring operative stabilization in most instances. This recommendation has been made with little biomechanical data to support it. The purpose of this study was to determine the osseous and ligamentous contributions to the stability of experimentally created scapular neck fractures in a cadaver model. METHODS: Standardized scapular neck fractures were made in twelve fresh-frozen human cadaveric shoulders. Each specimen was mounted in a specially designed testing apparatus and secured to a standard materials testing device. In group 1 (six shoulders), resistance to medial displacement was determined following sequential creation of an ipsilateral clavicular fracture, coracoacromial ligament disruption, and acromioclavicular capsular disruption. In group 2 (six shoulders), resistance to medial displacement was determined following sequential sectioning of the coracoacromial and coracoclavicular ligaments. RESULTS: The average measured force for all specimens (groups 1 and 2) after scapular neck fracture was 183 +/- 3.3 N (range, 166 to 203 N). The addition of a clavicular fracture (group 1) resulted in an average measured force of 128 +/- 10.5 N (range, 83 to 153 N), which corresponds to only a 30% loss of stability. Subsequent sectioning of the coracoacromial and acromioclavicular capsular ligaments yielded an average force of 126 +/- 9.1 N (range, 114 to 144 N), a 31% loss of stability, and 0 N, a complete loss of stability, respectively. Sectioning of the coracoacromial and coracoclavicular ligaments after scapular neck fracture (group 2) resulted in an average force of 103 +/- 8.4 N (range, 89 to 118 N), a 44% loss of stability, and 0 N, a complete loss of stability, respectively. CONCLUSIONS: Ipsilateral fractures of the scapular neck and the clavicular shaft do not produce a floating shoulder without additional disruption of the coracoacromial and acromioclavicular capsular ligaments. These and other unstable combined injury patterns are likely to be accompanied by substantial medial displacement of the glenoid fragment.

Aged↗
PubMed2006

Ultrastable substrates for surface-enhanced Raman spectroscopy: Al2O3 overlayers fabricated by atomic layer deposition yield improved anthrax biomarker detection.

A new method to stabilize and functionalize surfaces for surface-enhanced Raman spectroscopy (SERS) is demonstrated. Atomic layer deposition (ALD) is used to deposit a sub-1-nm alumina layer on silver film-over-nanosphere (AgFON) substrates. The resulting overlayer maintains and stabilizes the SERS activity of the underlying silver while presenting the surface chemistry of the alumina overlayer, a commonly used polar adsorbent in chromatographic separations. The relative affinity of analytes for alumina-modified AgFON substrates can be determined by their polarity. On the basis of SERS measurements, dipicolinic acid displays the strongest binding to the ALD alumina-modified AgFON among a set of pyridine derivatives with varying polarity. This strong affinity for carboxylate groups makes the SERS substrate an ideal candidate for bacillus spores detection using the dipicolinate biomarker. The SERS signal from extracted dipicolinate was measured over the spore concentration range 10(-14)-10(-12) M to determine the saturation binding capacity of the alumina-modified AgFON surface. The adsorption constant was determined to be Kspore = 9.0 x 10(13) M(-1). A 10-s data collection time is capable of achieving a limit of detection of approximately 1.4 x 10(3) spores. The shelf life of prefabricated substrates is at least 9 months prior to use. In comparison to the bare AgFON substrates, the ALD-modified AgFON substrates demonstrate twice the sensitivity with 6 times shorter data acquisition time and 7 times longer temporal stability. ALD expands the palette of available chemical methods to functionalize SERS substrates, which will enable improved and diverse chemical control over the nature of analyte-surface binding for biomedical, homeland security, and environmental applications.

Aluminum Oxide↗
PubMed1987

Changes in translational yield regulate tissue-specific expression of beta-glucuronidase.

The number of beta-glucuronidase (GUS; beta-D-glucuronoside glucuronosohydrolase, EC 3.2.1.31) molecules per cell varies as much as 12-fold among mouse tissues. To identify the regulatory mechanisms responsible, estimates of the rates of GUS protein synthesis (ks) and degradation (kd) were obtained for six tissues in the B6.PAC-Gusn mouse strain, which carries the N haplotype of the GUS gene. Differences in enzyme levels among tissues were predominantly due to differences in rates of enzyme synthesis; only brain differed significantly in the rate of protein degradation. Typically, tissues contain about 2 molecules of GUS mRNA per cell. Differences in GUS mRNA levels were found among tissues, but these were not sufficient to account for observed differences in ks. This suggests that tissues differ in translational yield, which is defined as the product of the efficiency with which the GUS message is translated and the fraction of newly made polypeptides that are successfully matured into GUS tetramers. Experimental estimates of translational yield confirmed that this is indeed a source of tissue differences in GUS gene regulation. This finding also proved to be true of the B haplotype of the GUS gene. The differential regulation of special-function genes is, in general, effected transcriptionally. In contrast, the differential regulation of several "housekeeping" genes has been reported to arise from changes in mRNA maturation and/or stability. It is now apparent that translational yield, which is an aspect of protein synthesis, can also serve as a differential regulatory mechanism.

Animals↗
PubMed1993

Effects of various cryoprotective agents and membrane-stabilizing compounds on bull sperm membrane integrity after cooling and freezing.

In this study attempts were made to improve the survival rates of bull spermatozoa after freezing/thawing and to clarify the importance of certain agents to the cryopreservation of spermatozoa. For that purpose the standard freezing extender was modified by the addition of different concentrations of various cryoprotectants and membrane-stabilizing agents: glycerol, 1,2-propanediol, polyvinylpyrrolidone, sucrose, egg yolk, lipid vesicles, and bovine serum albumin (BSA). Sperm membrane impermeability toward H33258 was employed as the parameter for sperm integrity during cooling and after freezing/thawing. Exclusion of glycerol from the extender did not significantly affect sperm integrity. Replacing 6% glycerol by 6% 1,2-propanediol resulted in reduced sperm survival, whereas replacement of glycerol by 62.5 mM sucrose slightly improved survival rates. Addition of 5 or 10% polyvinylpyrrolidone (either or not in combination with 0.5 M sucrose) significantly reduced sperm integrity. Excluding egg yolk from the extender caused a serious decrease of sperm survival after both cooling and freezing. The cryoprotection offered by egg yolk could not be mimicked by dioleoylphosphatidylcholine (DOPC) vesicles or DOPC/phosphatidic acid/cholesterol vesicles in concentrations up to 29 or 9 mM, respectively. However, the freezing extender containing 6.5 mM DOPC vesicles in combination with 6% BSA yielded results which did not significantly differ from those obtained with the standard extender; higher vesicle concentrations combined with BSA might produce even better results. Further research on the cryopreservation of bovine spermatozoa should focus on membrane stabilization since the membrane-stabilizing compounds yield more promising results than the ice-preventing agents.

Animals↗
PubMed1997

Stability, specificity and fluorescence brightness of multiply-labeled fluorescent DNA probes.

In this work, we studied the fluorescence and hybridization of multiply-labeled DNA probes which have the hydrophilic fluorophore 1-(straightepsilon-carboxypentynyl)-1'-ethyl- 3,3,3', 3'-tetramethylindocarbocyanine-5,5'-disulfonate (Cy3) attached via either a short or long linker at the C-5 position of deoxyuridine. We describe the effects of labeling density, fluorophore charge and linker length upon five properties of the probe: fluorescence intensity, the change in fluorescence upon duplex formation, the quantum yield of fluorescence (Phif), probe-target stability and specificity. For the hydrophilic dye Cy3, we have demonstrated that the fluorescence intensity andPhifare maximized when labeling every 6th base using the long linker. With a less hydrophilic dye, a labeling density this high could not be achieved without serious quenching of the fluorescence. The target specificity of multiply-labeled DNA probes was just as high as compared to the unmodified control probe, however, a less stable probe-target duplex is formed that exhibits a lower melting temperature. A mechanism that accounts for this destabilization is proposed which is consistent with our data. It involves dye-dye and dye-nucleotide interactions which appear to stabilize a single-stranded conformation of the probe.

Carbocyanines↗
PubMed1999

Laulimalide and isolaulimalide, new paclitaxel-like microtubule-stabilizing agents.

A mechanism-based screening program aimed at the discovery of new antimicrotubule agents from natural products yielded laulimalide and isolaulimalide, two compounds with paclitaxel-like microtubule-stabilizing activity. Treatment of A-10 cells with laulimalide resulted in a dose-dependent reorganization of the cellular microtubule network and the formation of microtubule bundles and abnormal mitotic spindles. Coincident with the microtubule changes, these two compounds induced nuclear convolution and the formation of multiple micronuclei. Laulimalide is a potent inhibitor of cellular proliferation with IC50 values in the low nanomolar range, whereas isolaulimalide is much less potent with IC50 values in the low micromolar range. In contrast to paclitaxel, both laulimalide and isolaulimalide inhibited the proliferation of SKVLB-1 cells, a P-glycoprotein overexpressing multidrug-resistant cell line, suggesting that they are poor substrates for transport by P-glycoprotein. Incubation of MDA-MB-435 cells with laulimalide resulted in mitotic arrest and activation of the caspase cascade of proteolytic enzymes that accompany apoptotic cell death. Laulimalide stimulated tubulin polymerization and, although less potent than paclitaxel, it was more effective. Laulimalide-induced tubulin polymers resembled paclitaxel-induced polymers, although the laulimalide-induced polymers appeared notably longer. Laulimalide and isolaulimalide represent a new class of microtubule-stabilizing agents with activities that may provide therapeutic utility.

Animals↗
PubMed2002

Stability scale and atomic solvation parameters extracted from 1023 mutation experiments.

The stability scale of 20 amino acid residues is derived from a database of 1023 mutation experiments on 35 proteins. The resulting scale of hydrophobic residues has an excellent correlation with the octanol-to-water transfer free energy corrected with an additional Flory-Huggins molar-volume term (correlation coefficient r = 0.95, slope = 1.05, and a near zero intercept). Thus, hydrophobic contribution to folding stability is characterized remarkably well by transfer experiments. However, no corresponding correlation is found for hydrophilic residues. Both the hydrophilic portion and the entire scale, however, correlate strongly with average burial accessible surface (r = 0.76 and 0.97, respectively). Such a strong correlation leads to a near uniform value of the atomic solvation parameters for atoms C, S, O/N, O(-0.5), and N(+0.5,1). All are in the range of 12-28 cal x mol(-1) A(-2), close to the original estimate of hydrophobic contribution of 25-30 cal x mol(-1) A(-2) to folding stability. Without any adjustable parameters, the new stability scale and new atomic solvation parameters yielded an accurate prediction of protein-protein binding free energy for a separate database of 21 protein-protein complexes (r = 0.80 and slope = 1.06, and r = 0.83 and slope = 0.93, respectively).

Amino Acids↗
PubMed1996

Effect of additives on the renaturation of reduced lysozyme in the presence of 4 M urea.

Reduced lysozyme was renatured by sulfhydryl-disulfide interchange reactions at pH 8.0 in the presence of 4 M urea, with or without additives at 40 degrees C. In the absence of additives, the final folding yield of reduced lysozyme was approximately 40%. In the presence of sarcosine, glycerol, ammonium sulfate, N-acetyl glucosamine and glucose, its folding yields increased in all cases. In particular, yields increased up to 90% in the presence of 4 M sarcosine. On the other hand, the melting temperatures of lysozyme with or without additives in 0.02 M citrate buffer (pH 6.0) were evaluated using differential scanning calorimetry. In the absence of additive, the melting temperature of lysozyme was 73.8 degrees C. In the presence of additives, all melting temperatures were higher than that of lysozyme in the absence of additives. Moreover, there was a good correlation on addition of additives between an increase in the folding yield of reduced lysozyme with 4 M urea and an increase in the melting temperature without 4 M urea. Therefore, we conclude that additives, which stabilize native lysozyme, are effective at increasing the folding yield of reduced lysozyme in 4 M urea.

Acetylglucosamine↗
PubMed2006

Deterministic, compensatory mutational events in the capsid of foot-and-mouth disease virus in response to the introduction of mutations found in viruses from persistent infections.

The evolution of foot-and-mouth disease virus (FMDV) (biological clone C-S8c1) in persistently infected cells led to the emergence of a variant (R100) that displayed increased virulence, reduced stability, and other modified phenotypic traits. Some mutations fixed in the R100 genome involved a cluster of highly conserved residues around the capsid pores that participate in interactions with each other and/or between capsid protomers. We have investigated phenotypic and genotypic changes that occurred when these replacements were introduced into the C-S8c1 capsid. The C3007V and M3014L mutations exerted no effect on plaque size or viral yield during lytic infections, or on virion stability, but led to a reduction in biological fitness; the D3009A mutation caused drastic reductions in plaque size and viability. Remarkably, competition of the C3007V mutant with the nonmutated virus invariably resulted in the fixation of the D3009A mutation in the C3007V capsid. In turn, the presence of the D3009A mutation invariably led to the fixation of the M3014L mutation. In both cases, two individually disadvantageous mutations led, together, to an increase in fitness, as the double mutants outcompeted the nonmutated genotype. The higher fitness of C3007V/D3009A was related to a faster multiplication rate. These observations provide evidence for a chain of linked, compensatory mutational events in a defined region of the FMDV capsid. Furthermore, they indicate that the clustering of unique amino acid replacements in viruses from persistent infections may also occur in cytolytic infections in response to changes caused by previous mutations without an involvement of the new mutations in the adaptation to a different environment.

Adaptation, Physiological↗
PubMed2001

Reactor optimization for alpha-1,2 glucooligosaccharide synthesis by immobilized dextransucrase.

The immobilization of dextransucrase in Ca-alginate beads relies on the close association between dextran polymer and dextransucrase. However, high amounts of dextran in the enzyme preparation drastically limit the specific activity of the immobilized enzyme (4 U/mL of alginate beads). Moreover, even in the absence of diffusion limitation at the batch conditions used, the enzyme behavior is modified by entrapment so that the dextran yield increases and the alpha-1,2 glucooligosaccharides (GOS) are produced with a lower yield (46.6% instead of 56.7%) and have a lower mean degree of polymerization than with the free dextransucrase. When the immobilized catalyst is used in a continuous reaction, the reactor flow rate necessary to obtain high conversion of the substrates is very low, leading to external diffusion resistance. As a result, dextran synthesis is even higher than in the batch reaction, and its accumulation within the alginate beads limits the operational stability of the catalyst and decreases glucooligosaccharide yield and productivity. This effect can be limited by using reactor columns with length to diameter ratio > or =20, and by optimizing the substrate concentrations in the feed solution: the best productivity obtained was 3.74 g. U(-1). h(-1), with an alpha-1,2 GOS yield of 36%.

Bioreactors↗
PubMedDate not supplied

The purification and properties of monoacylglycerol kinase from bovine brain.

Monoacylglycerol kinase (MGK) has been purified from bovine brain by six steps: isolation of cytosol, DEAE-cellulose chromatography, ammonium sulfate fractionation (0-40%), Bio-Gel A-1.5m, hydroxylapatite, and ATP-agarose column chromatography. The overall purification was 938 times with a 4.8% yield. The column separations (particularly Bio-Gel A-1.5m) and SDS- and nondenaturing-polyacrylamide gel electrophoresis of enzyme purified from ATP-agarose indicated that MGK exists as a complex (approximately 350 kilodaltons) that is stabilized by 0.5 M NaCl and, on complete dissociation, yields a major protein of 72 kilodaltons. Dithiothreitol, EDTA, and ATP helped to stabilize MGK during purification. The protein peak eluted from hydroxylapatite by 25 mM phosphate activated and stabilized MGK activity. Phosphatidylcholine, phosphatidylethanolamine, and sphingomyelin inhibited MGK. These phospholipids and others activated MGK synergistically with the above protein peak. MGK copurified with diacylglycerol kinase (DGK) throughout giving MGK to DGK ratios of 0.05-0.36. Optimal activity required 0.5 mM 2-monoolein and 10 mM MgCl2. Strong inhibition by p-chloromercuriphenyl sulfonic acid, N-ethyl-maleimide, and 5,5'-dithio-bis(2-nitrobenzoic acid), and prevention of this inhibition by dithiothreitol indicated the involvement of intact SH groups in the action of MGK. Purified MGK showed preference for substrates with unsaturated fatty acids except for 1- or 2-monostearin. Overall the preference favored the selective generation of 1-stearoyl- and 2-arachidonoyl-lysophosphatidic acid.

Animals↗
PubMed2002

Protein S1 counteracts the inhibitory effect of the extended Shine-Dalgarno sequence on translation.

There are two major components of Escherichia coli ribosomes directly involved in selection and binding of mRNA during initiation of protein synthesis-the highly conserved 3' end of 16S rRNA (aSD) complementary to the Shine-Dalgarno (SD) domain of mRNA, and the ribosomal protein S1. A contribution of the SD-aSD and S1-mRNA interactions to translation yield in vivo has been evaluated in a genetic system developed to compare efficiencies of various ribosome-binding sites (RBS) in driving beta-galactosidase synthesis from the single-copy (chromosomal) lacZ gene. The in vivo experiments have been supplemented by in vitro toeprinting and gel-mobility shift assays. A shortening of a potential SD-aSD duplex from 10 to 8 and to 6 bp increased the beta-galactosidase yield (four- and sixfold, respectively) suggesting that an extended SD-aSD duplex adversely affects translation, most likely due to its redundant stability causing ribosome stalling at the initiation step. Translation yields were significantly increased upon insertion of the A/U-rich S1 binding targets upstream of the SD region, but the longest SD remained relatively less efficient. In contrast to complete 30S ribosomes, the S1-depleted 30S particles have been able to form an extended SD-aSD duplex, but not the true ternary initiation complex. Taken together, the in vivo and in vitro data allow us to conclude that S1 plays two roles in translation initiation: It forms an essential part of the mRNA-binding track even when mRNA bears a long SD sequence, and through the binding to the 5' untranslated region, it can ensure a substantial enhancing effect on translation.

5' Untranslated Regions↗
PubMed2006

Growth of gold nanorods and bipyramids using CTEAB surfactant.

Gold nanorods and bipyramids have been synthesized using the seed-mediated approach in aqueous cetyltriethylammonium bromide (CTEAB) solutions in the presence of silver nitrate. Gold nanoparticle seeds that are stabilized with either CTEAB or sodium citrate have been used. The use of the CTEAB-stabilized seeds gives gold nanorods in high yield in one step with the longitudinal plasmon wavelength ranging from 750 to 1030 nm, depending on the amount of the seeds. The longitudinal plasmon wavelength can be extended to 1100 nm by the use of a two-step growth method. The growth of gold nanorods in CTEAB solutions takes 5-10 h, more than 5 times slower than that in cetyltrimethylammonium bromide solutions at the same concentration of surfactants. The use of the citrate-stabilized seeds gives both gold bipyramids and a small percentage of gold nanorods. The longitudinal plasmon wavelength of the bipyramids is tunable from 700 to 1100 nm by varying the amount of the citrate-stabilized seeds. The growth of gold bipyramids takes more than 1 day. Transmission electron microscopy characterizations reveal that the gold nanorods grown from both types of gold nanoparticle seeds are single-crystalline and that the gold bipyramids are penta-twinned.

Journal Article↗
PubMed1999

Activity-stability considerations of trypsinogen during spray drying: effects of sucrose.

The preparation and processing of protein pharmaceuticals into powders may impose significant stresses that could perturb and ultimately denature them. In many cases their stabilization through added excipients is necessary to yield native and active proteins. In this study, the effect of spray drying on the structure and activity of a model protein (trypsinogen) was investigated. In the absence of excipients, spray drying resulted in small losses of its enzymatic activity. Protein conformational rearrangements in the solid state (observed via FTIR) and irreversible aggregation (upon reconstitution) constituted the major degradation pathways. The irreversible unfolding in the solid state was also confirmed by solution calorimetric studies that indicated a decreased thermal stability of the spray-dried protein after reconstitution. The presence of sucrose, a thermal and dehydration stress stabilizer, induced a concentration-dependent protective effect. Protein protection was afforded even at low carbohydrate concentrations, while at specific mass ratios (sucrose-to-protein = 1:1) complete activity preservation was achieved. However, at the high end of sucrose concentrations, a small destabilization was evident, indicating that excluded volume effects may be undesirable during preparation of protein microparticles via spray drying. The profile of both the protein conformational changes and thermal stability in the solid state closely followed that of the incurred activity losses, indicating that protein stabilization during dehydration is crucial during processing of these polypeptides.

Chemistry, Pharmaceutical↗