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At least 289 records · Page 16Linked to original sources
PubMed2003

Expression of heteropolymeric ferritin improves iron storage in Saccharomyces cerevisiae.

Saccharomyces cerevisiae was engineered to express different amount of heavy (H)- and light (L)-chain subunits of human ferritin by using a low-copy integrative vector (YIp) and a high-copy episomal vector (YEp). In addition to pep4::HIS3 allele, the expression host strain was bred to have the selection markers leu2(-) and ura3(-) for YIplac128 and YEp352, respectively. The heterologous expression of phytase was used to determine the expression capability of the host strain. Expression in the new host strain (2805-a7) was as high as that in the parental strain (2805), which expresses high levels of several foreign genes. Following transformation, Northern and Western blot analyses demonstrated the expression of H- and L-chain genes. The recombinant yeast was more iron tolerant, in that transformed cells formed colonies on plates containing more than 25 mM ferric citrate, whereas none of the recipient strain cells did. Prussian blue staining indicated that the expressed isoferritins were assembled in vivo into a complex that bound iron. The expressed subunits showed a clear preference for the formation of heteropolymers over homopolymers. The molar ratio of H to L chains was estimated to be 1:6.8. The gel-purified heteropolymer took up iron faster than the L homopolymer, and it took up more iron than the H homopolymer did. The iron concentrations in transformants expressing the heteropolymer, L homopolymer, and H homopolymer were 1,004, 760, and 500 micro g per g (dry weight) of recombinant yeast cells, respectively. The results indicate that heterologously expressed H and L subunits coassemble into a heteropolymer in vivo and that the iron-carrying capacity of yeast is further enhanced by the expression of heteropolymeric isoferritin.

6-Phytase↗
PubMed2005

A modular approach toward block copolymers.

A novel methodology for the formation of block copolymers has been developed that combines ring-opening metathesis polymerization (ROMP) with functional chain-transfer agents (CTAs) and self-assembly. Telechelic homopolymers of cyclooctene derivatives end-functionalized with hydrogen-bonding or metal-coordination sites are formed through the combination of ROMP with a corresponding functional CTA. These telechelic homopolymers are fashioned with a high control over molecular weight and without the need for post-polymerization procedures. The homopolymers undergo fast and efficient self-assembly with their complement homopolymer or small molecule analogue to form block-copolymer architectures. The block copolymers show equivalent association constants as their small molecule analogues described in the literature, regardless of size or nature of the complementary unit or the polymer side chain.

Carbon↗
PubMed1998

Formation and movement of Fe(III) in horse spleen, H- and L-recombinant ferritins. A fluorescence study.

Iron oxidation and incorporation into apoferritins of different subunit composition, namely the recombinant H and L homopolymers and the natural horse spleen heteropolymer (10-15% H), have been followed by steady-state and time-resolved fluorescence. After aerobic addition of 100 Fe(II) atoms/polymer, markedly different kinetic profiles are observed. In the rL-homopolymer a slow monotonic fluorescence quenching is observed which reflects binding, slow oxidation at the threefold apoferritin channels, and diffusion into the protein cavity. In the rH-homopolymer a fast fluorescence quenching is followed by a partial, slow recovery. The two processes have been attributed to Fe(II) binding and oxidation at the ferroxidase centers and to Fe(III) released into the cavity, respectively. The fluorescence kinetics of horse spleen apoferritin is dominated by the H chain contribution and resembles that of the H homopolymer. It brings out clearly that the rate of the overall process is limited by the rate at which Fe(III) leaves the ferroxidase centers of the H chains where binding of incoming Fe(II) and its oxidation take place. The data obtained upon stepwise addition of iron and the results of optical absorption measurements confirm this picture. The correspondence between steady-state and time-resolved data is remarkably good; this is manifest when the latter are used to calculate the change in fluorescence intensity as apparent in the steady-state measurements.

Animals↗
PubMed2003

Polymer complexes. XXXX. Supramolecular assembly on coordination models of mixed-valence-ligand poly[1-acrylamido-2-(2-pyridyl)ethane] complexes.

The build-up of polymer metallic supramolecules based on homopolymer (1-acrylamido-2-(2-pyridyl)ethane (AEPH)) and ruthenium, rhodium, palladium as well as platinum complexes has been pursued with great interest. The homopolymer shows three types of coordination behaviour. In the mixed valence paramagnetic trinuclear polymer complexes [(11)+(12)] in the paper and in mononuclear polymer complexes (1)-(5) it acts as a neutral bidentate ligand coordinating through the N-pyridine and NH-imino atoms, while in the mixed ligand diamagnetic poly-chelates, which are obtained from the reaction of AEPH with PdX2 and KPtCl4 in the presence of N-heterocyclic base consisting of polymer complexes (9)+(10), and in monouclear compounds (6)-(8), it behaves as a monobasic bidentate ligand coordinating through the same donor atoms. In mononuclear compounds (13)+(14) it acts as a monobasic and neutral bidentate ligand coordinating only through the same donor atoms. Monomeric distorted octahedral or trimeric chlorine-bridged, approximately octahedral structures are proposed for these polymer complexes. The poly-chelates are of 1:1, 1:2 and 3:2 (metal-homopolymer) stoichiometry and exhibit six coordination. The values of ligand field parameters were calculated. The homopolymer and their polymer complexes have been characterized physicochemically.

Chelating Agents↗
PubMed1997

Temperature-responsive liquid chromatography. 2. Effects of hydrophobic groups in N-isopropylacrylamide copolymer-modified silica.

We recently reported the new concept of temperature-responsive liquid chromatography using temperature-responsive poly(N-isopropylacrylamide)-modified surfaces as high-performance liquid chromatography media with aqueous mobile phases. Incorporation of hydrophobic sites is an important factor to improve the efficacy (selectivity and retention) of temperature-responsive chromatography. Toward this goal, we have synthesized semitelechelic copolymers of N-isopropylacrylamide (IPAAm) and butyl methacrylate (BMA) having reactive terminal functional groups using telomerization. The lower critical solution temperatures of the copolymers shift to lower temperatures with increasing hydrophobic BMA content in the poly(IPAAm-co-BMA) relative to that of the IPAAm homopolymer. This temperature-responsive semitelechelic copolymer was grafted to the surface of (aminopropyl)silica through the reaction of activated ester-amine coupling. The polymer-modified silica was used as a column packing material. Separation of a mixture of five steroids having various hydrophobicities was investigated. Retention of steroids on poly(IPAAm-co-BMA)-modified columns is increased with an increase in column temperature. The capacity factors for steroids on the copolymer-modified silica beads was much larger than that on homopolymer PIPAAm-modified columns. The capacity factor for testosterone at 50 degrees C was 33.8 for poly(IPAAm-co-BMA) containing 5 mol% BMA, while that for the PIPAAm homopolymer was 15.0 at the same temperature. The influence of column temperature on steroid retention behavior on copolymer-modified stationary phases was significant compared with the case of homopolymer-modified columns. Furthermore, retention times for steroids increased remarkably with increasing BMA composition. The temperature-responsive elution behavior for the steroids was strongly affected by the hydrophobicity of the grafted polymer chains on silica surfaces. Possible protein separation in temperature-responsive liquid chromatography was explored using insulin chains A and B, and beta-endorphin fragment 1-27. On IBc-3.2-modified silica column, these three peptides were successfully separated at 30 degrees C with 0.5 M NaCl aqueous solution (pH 2.1) as mobile phase. The retention times of these peptides were related to the number of hydrophobic amino acid residues in the peptides. In the proposed chromatography system, elution of target substances is controlled only by a small change in column temperature without any further modification of the aqueous mobile phase.

Acrylamides↗
PubMed1981

Structure, assembly, conformation, and immunological properties of the two subunit classes of ferritin.

The two subunit types of human liver ferritin were purified to homogeneity. Both subunits reassembled in a well-defined manner and formed spherical particles that resembled natural apoferritin in electron micrographs. Affinity chromatography methods were employed to obtain preparations of antibodies that interacted exclusively either with the H or with the L polypeptides, demonstrating that distinct immunological properties may be ascribed to each subunit of ferritin. The amino acid compositions of the subunits were similar, but the larger H subunit had fewer leucine, phenylalanine, and arginine residues. It is therefore improbable that H subunits undergo proteolytic processing and are precursors for L subunits. Circular dichroism data indicated that homopolymers assembled from L-type subunits had substantially more ordered secondary structures and greater alpha-helical contents than their H counterparts. Small differences in the environment of tryptophan residues were evident from fluorescence spectra of each homopolymer. In isoelectric focusing experiments reassembled H or L homopolymers migrated as families of proteins within discrete pI ranges which are probably representative of subpopulations of each subunit type. The H homopolymer focused at lower pI's than the L component. These data substantiate the contention that both subunits are authentic polypeptide moieties of ferritin with some common structural features, but the results also underscore prominent dissimilarities in their properties.

Apoferritins↗
PubMed2006

Design of random copolymers with statistically controlled monomer sequence distributions via Monte Carlo simulations.

We use Monte Carlo simulations to model the formation of random copolymers with tunable monomer sequence distributions. Our scheme is based on the original idea proposed a few years ago by Khokhlov and Khalatur [Physica A 249, 253 (1998); Phys. Rev. Lett. 82, 3456 (1999)], who showed that the distribution of species B in A-B random copolymers can be regulated by (a) adjusting the coil size of a homopolymer A and (b) chemically modifying ("coloring") monomers that reside at (or close to) the periphery of the coil with species B. In contrast to Khokhlov and Khalatur's work, who modeled the polymer modification by performing the coloring instantaneously, we let the chemical coloring reaction progress over time using computer simulations. We show that similar to Khokhlov and Khalatur's work, the blockiness (i.e., number of consecutive monomers) of the B species along the A-B copolymer increases with increasing degree of collapse of the parent homopolymer A. A simple analysis of the A-B monomer sequences in the copolymers reveals that monomer sequence distributions in homopolymers "colored" under collapsed conformations possess certain degrees of self-similarity, while there is no correlation found among the monomer sequence distributions formed by coloring homopolymers with expanded conformations.

Journal Article↗
PubMed1991

The number of positively charged amino acids in the basic domain of Tat is critical for trans-activation and complex formation with TAR RNA.

The basic domain of Tat is required for trans-activation of viral gene expression. We have performed scanning peptide studies to demonstrate that only this domain is capable of binding to the TAR RNA stem-loop. Strikingly, the basic domain of the other human immunodeficiency virus trans-acting factor, Rev, but no other region, is also capable of binding to TAR. Peptide derivatives of Tat do not require the highly conserved glutamine residue at position 54 for TAR binding, since it may be substituted or deleted. In addition, the two lysine residues may be replaced by arginines. Analysis of binding and trans-activation demonstrated that homopolymers of arginine can completely substitute for the basic domain. Such homopolymers have high affinity for wild-type TAR RNA and lower affinity for mutant TAR. Homopolymers of six to nine arginines substituting for the basic domain of Tat enable full trans-activation in vivo. Homopolymers of at least seven arginines are required for detectable in vitro complex formation, although approximately 30% trans-activation is achieved with a mutant Tat containing only five arginines.

Amino Acid Sequence↗
PubMed1996

Aquatic risk assessment of a polycarboxylate dispersant polymer used in laundry detergents.

Polycarboxylates enhance detergent soil removal properties and prevent encrustation of calcium salts on fabrics during washing. Laundry wastewater typically reaches wastewater treatment plants, which then discharge into aquatic environments. The yearly average concentration of a 4500 molecular weight (MW) sodium acrylate homopolymer reaching U.S. wastewater treatment plants will be approximately 0.7 mg/L. Publications showing the low to moderate acute aquatic toxicity of polycarboxylates are readily available. However, there are no published evaluations that estimate wastewater removal and characterize the probability of exceedance of acceptable chronic aquatic exposure. WW-TREAT can be used to estimate removal during wastewater treatment and PG-GRIDS can be applied to characterize risk for exceedance in wastewater treatment plant outfalls. After adjustments for the MW distribution of the homopolymer, WW-TREAT predicted that 6.5% will be removed in primary treatment plants and 60% will be removed in combined primary and activated sludge treatment plants. These estimates are consistent with wastewater fate tests, but underestimate homopolymer removal when homopolymer precipitation is included. Acceptable levels of chronic outfall (receiving water) exposure were based on aquatic toxicity testing in algae, fish, and Daphnia magna. PG-GRIDS predicted that no unreasonable risk for exceedance of acceptable chronic exposure will occur in the outfalls of U.S. wastewater plants. Future development of wastewater treatment models should consider polymer MW distribution and precipitation as factors that may alter removal of materials from wastewater.

Acrylates↗
PubMed1987

The thermodynamics of drug-DNA interactions: ethidium bromide and propidium iodide.

We report the first calorimetrically-derived characterization of the thermodynamics of ethidium bromide (EB) and propidium iodide (PI) binding to a series of nucleic acid host duplexes. Our spectroscopic and calorimetric measurements yield the following results: 1) At low salt (16mM Na+) and 25 degrees C. PI binds more strongly than EB to a given host duplex. The magnitude of this PI preference depends only marginally on base sequence, with AT base pairs showing a greater PI preference than GC base pairs. 2) The enhanced binding of PI relative to EB at low salt and 25 degrees C reflects a more favorable entropic driving force for PI binding. 3) The PI binding preference diminishes at higher salt concentrations (216mM). In other words, the binding preference is electrostatic in origin. 4) The salt dependence of the binding constants (delta lnKb/delta ln[Na+]) reveal that PI binds as a dication while EB binds as a monocation. 5) PI and EB both exhibit impressive enthalpy-entropy compensations when they bind to the deoxy homopolymers poly dA.poly dT and poly dA.poly dU. We have observed a similar enthalpy-entropy compensation for netropsin binding to the poly dA.poly dT homopolymer duplex. We therefore conclude that the compensation phenomenon is an intrinsic property of the host duplex rather than reflecting a property of the binding ligand. 6) When either PI or EB bind to the corresponding ribo homopolymer (poly rA.poy rU) we do not observe the enthalpy-entropy compensation that characterizes the binding to the deoxy homopolymer. 7) EB and PI both bind more strongly to poly d(AT).poly d(AT) than to poly d(AU).poly d(AU). Specifically, the absence of the thymine methyl group in poly d(AU).poly d(AU) reduces the binding constant of both drugs by a factor of four. This reduction in binding is due to a less favorable entropy change. In this paper we present and discuss possible molecular origins for our observed thermodynamic and extra-thermodynamic data. In particular, we evoke solvent effects involving both the drugs and the host duplexes when we propose molecular interpretations which are consistent with our thermodynamic data.

Calorimetry, Differential Scanning↗
PubMed2006

Evidence for long poly(dA).poly(dT) tracts in D. discoideum DNA at high frequencies and their preferential avoidance of nucleosomal DNA core regions.

The eukaryote, Dictyostelium discoideum, has one of the most (A+T) rich genomes studied to date. Isolated nuclear D. discoideum DNA (AX3 strain) was used to qualitatively determine the frequency and length distribution of long (dA).(dT) homopolymer tracts in this genome, in comparison to the less (A+T) rich calf thymus and Schistosoma mansoni DNAs that had few observable long tracts. These experimental data accurately reflect the significantly elevated frequencies of long tracts found computationally within the D. discoideum intron and flanking sequences, but not exons. PCR amplification of long (dA).(dT) homopolymer tract containing sequences was carried out. Then experimental biotinylated (dT)18 probe hybridization to the PCR amplified DNA showed that the long (dA).(dT) homopolymer tracts were enriched in D. discoideum sequences only hundreds of base pair in length, under conditions where no equivalent hybridization was observed to S. mansoni DNA or calf DNA sequences. Similar probe hybridization to DNA isolated following micrococcal nuclease digestion of D. discoideum chromatin demonstrated that long (dA).(dT) homopolymer tracts were more highly enriched in nucleosomal DNA lengths that included the internucleosomal linker as compared to shorter linker free mononucleosomal lengths. This observation is in agreement with the frequency of tract spacing results calculated from GenBank sequence data. These frequency data indicate that adjacent long tracts plus the intervening spacer DNA are found at peak lengths (average 42 bp), exactly characteristic of the internucleosomal spacer region of D. discoideum chromatin and are in sufficient number to be found in nearly half of all nucleosomes. Compared to shuffled tract sequence controls, these lengths of adjacent long tracts plus the intervening spacer DNA were found to be significantly enriched. Lesser enrichments are observed at lengths corresponding to adjacent tracts being separated by nucleosomal core length DNA sequences (145-185 bp). These data strongly suggest that adjacent long tracts occur spaced at selected lengths so as to avoid the central core regions of nucleosomes and instead are found localized within internucleosomal DNA linker and core edge regions in D. discoideum chromatin.

Animals↗
PubMed1992

Serological cross-reaction between intact and chemically modified lipopolysaccharides of O1 Vibrio cholerae Inaba and non-O1 V. cholerae bio-serogroup Hakata.

Serological cross-reaction of intact as well as chemically modified LPS from O1 Vibrio cholerae 569B (Inaba) with non-O1 V. cholerae Hakata LPS, which contain alpha(1-->2)-linked N-acetyl perosamine-homopolymer constituting their O polysaccharide chain, was studied by passive hemolysis test by using their LPS as antigen for sensitizing sheep red blood cells (SRBC). The N-deacylation of the alpha(1-->2)-linked linear 3-deoxy-tetronyl perosamine-homopolymer constituting the O polysaccharide chain in 569B LPS resulted in virtual elimination of their serological reactivity with both homologous Inaba and heterologous Hakata antisera. Furthermore, when the resultant NH2 groups of the N-deacylated perosamine-homopolymers in 569B LPS were N-acylated with acetyl, propionyl or butanoyl groups, they markedly recovered the serological reactivity to a marked extent, in particular, their pronounced cross-serological reactivity with heterologous Hakata antiserum. These results are believed to be compatible with the interpretation that the Inaba antigen factor C possessed by the two bacteria studied is related to the common occurrence of the N-acyl groups, regardless of what the acyl groups are, residing in the perosamine residues of the perosamine-homopolymers constituting the O polysaccharide chain of their LPS.

Acetylation↗
PubMed1995

Immunochemistry of group A and Inaba C antigen factors constituting the O antigen of O1 Vibrio cholerae.

Serological cross-reactivity among intact lipopolysaccharides (LPS) from O1 Vibrio cholerae Inaba O-form (Inaba), Yersinia enterocolitica O9 (O9), non-O1 V. cholerae serogroup Hakata (Hakata) and Vibrio bio-serogroup 1875 Variant (1875 Variant) (all of which share Inaba antigen factor C), as well as a total of six kinds of chemically modified LPS (three from O9 and three from Inaba) was demonstrated by passive hemolysis and passive hemolysis inhibition by using these LPS as antigen for sensitizing sheep red blood cells and as inhibitor. These intact as well as chemically modified LPS contained, in their O polysaccharide chain, alpha(1-->2)-linked linear perosamine (4-amino-4,6-dideoxy-D-manno-pyranose) homopolymers with different N-acyl groups: their acyl groups comprise 3-deoxy-L-glycero-tetronyl (Inaba LPS), formyl (O9 LPS), 3-hydroxypropionyl (1875 Variant LPS), acetyl (Hakata LPS and artificially introduced into Inaba and O9 LPS), propionyl and butyryl (both artificially introduced into Inaba and O9 LPS) groups. N-Deacylation of the alpha(1-->2)-linked N-(3-deoxy-L-glycero-tetronyl)perosamine homopolymer of Inaba and the N-formyl one of O9 LPS resulted in virtual elimination of their serological reactivity with both homologous and heterologous antisera. Furthermore, when the resultant NH2 groups of the N-deacylated perosamine homopolymers of both LPS were N-acylated with acetyl, propionyl or butyryl groups, they markedly recovered both of their serological reactivities. These results are compatible with the interpretation that the Inaba antigen factor C possessed by the four bacteria is substantially related to the common presence of N-acyl groups, regardless of their identity, residing in the perosamine residues constituting the O polysaccharide chain of their LPS. It was also indicated that the group antigen factor A of O1 V. cholerae is substantially related to the 3-deoxy-L-glycero-tetronyl groups residing in the perosamine homopolymer of Inaba LPS.

Antibodies, Bacterial↗
PubMed1983

The interaction in vitro of the intermediate filament protein vimentin with synthetic polyribo- and polydeoxyribonucleotides.

In a continuation of our studies on the association of the intermediate filament protein vimentin with unfolded ribosomal subunits, rRNA and various naturally occurring RNAs and DNAs, we have investigated the binding of vimentin to a variety of synthetic polyribo- and polydeoxyribonucleotides. The vimentin-binding potentials of the different nucleic acids were determined in competition with 28S rRNA from Ehrlich ascites tumor cells. The reaction products were analysed by sucrose gradient centrifugation at low ionic strength and in the presence of EDTA. Among the homopolynucleotides tested, poly(rG), poly(rX), poly(rI), poly(rs4U) and poly(dG) were very good competitors, whereas poly(dC) was moderately so. Poly(rA), poly(rU), poly(rC), poly(dA), poly(dU), poly(dT) and poly(dI) were very weak competitors. Annealing of the active homopolymers to their complementary homopolymer strands resulted in a reduction of the vimentin-binding potential; however, the resulting duplexes still had substantial vimentin-binding capacity. A similar reduction was observed when the mononucleotides of the active homopolymers were randomly copolymerized with their complementary nucleotides or incorporated into strictly alternating, double-stranded DNAs. DNA-type copolymers, duplexes and alternating copolymers containing the nuclear bases adenine, thymine and uracil were moderate competitors, but, in general, they were significantly more active than the corresponding homopolymers. This result, together with those of the analysis of a series of random heteropolyribonucleotides, indicates that there is some influence of the base sequence and/or secondary structure of the nucleic acids on their vimentin-binding capacities. Whereas the minimum length of oligo(dG) for efficient vimentin binding was between 11 and 18 nucleotides, (dT)18 was still incapable of interacting with vimentin. In order to obtain information on the salt stability of vimentin-nucleic acid adducts, we have also performed affinity chromatographies on single-stranded calf thymus DNA-cellulose and on rRNA and homopolyribonucleotides covalently coupled to agarose. Although because of unspecific secondary interaction of vimentin with the matrix, these nucleic acid-substituted absorbents could not be used for this purpose under non-denaturing conditions, in the presence of 6M urea a relationship between the nucleic acid substitution and the salt stability of vimentin binding was observed. Finally, the nucleic acid-binding properties of vimentin are compared with those of cytosolic steroid hormone receptors, particularly with those of the androgen receptor.

Animals↗
PubMed1989

In vitro and ex vivo platelet interactions with hydrophilic-hydrophobic poly(ethylene oxide)-polystyrene multiblock copolymers.

Hydrophilic-hydrophobic multiblock copolymers synthesized from telechelic oligomers of poly(ethylene oxide) (PEO) and polystyrene (PS) have been used to study the influence of hydrophilic and hydrophobic balance on interfacial interactions of these surfaces with blood components. In vitro coagulation assays show no inherent ability of these amphiphilic surfaces to affect contact activation or coagulation factors. In vitro platelet adhesion and release reactions from rabbit platelet-rich plasma were shown to be greatest on Biomer and PS homopolymer surfaces and least on cross-linked PEO surfaces, with the PEO-PS block copolymers demonstrating intermediate responses. These same substrates were tested in a new low-flow, low-shear arterio-artery shunt system in rabbits. Whole blood occlusion times were not a direct function of hydrophilic content as both PEO and PS homopolymers and Biomer showed short occlusion times, while PEO-PS block copolymers prolonged occlusion times considerably, depending on composition. Overall, results suggest that PEO-PS block copolymers promote unique whole blood responses in contrast to homopolymer and Biomer controls which are more complex than direct correlations to bulk hydrophilic and hydrophobic contents.

Anastomosis, Surgical↗
PubMed2004

Degradation and cell culture studies on block copolymers prepared by ring opening polymerization of epsilon-caprolactone in the presence of poly(ethylene glycol).

Poly(epsilon-caprolactone) (PCL) and its block copolymers with poly(ethylene glycol) (PEG) were prepared by ring-opening polymerization of epsilon-caprolactone in the presence of ethylene glycol or PEG, using zinc metal as catalyst. The resulting polymers were characterized by various analytical techniques such as (1)H NMR, SEC, DSC, IR, X-ray, ESEM, and CZE. PCL/PEG copolymers with long PCL chains presented the same crystalline structure as PCL homopolymer, whereas PEG-bearing short PCL blocks retained the crystalline structure of PEG and exhibited an amphiphilic behavior in aqueous solutions. Degradation of PCL and PCL/PEG diblock and triblock copolymers was realized in a 0.13 M, pH 7.4 phosphate buffer at 37 degrees C. The results indicated that the copolymers exhibited higher hydrophilicity and degradability compared with the PCL homopolymer. Large amounts of PEG were released from the bulk after 60 weeks' degradation. In vitro cell culture studies were conducted on scaffolds manufactured via solid free form fabrication by using primary human and rat bone marrow derived stromal cells (hMSC, rMSC). Light, scanning electron, and confocal laser microscopy, as well as immunocytochemistry, showed cell attachment, proliferation, and extracellular matrix production on the surface, as well as inside the scaffold architecture. Copolymers showed better performance in the cell culture studies than the PCL homopolymer.

Animals↗
PubMed2006

Study on blood compatibility with poly(2-methoxyethylacrylate)--relationship between surface structure, water structure, and platelet compatibility in 2-methoxyethylacrylate/2-hydroxyethylmethacrylate diblock copolymer.

Diblock copolymers composed of 2-methoxyethylacrylate (MEA) and 2-hydroxyethylmethacrylate (HEMA) were firstly prepared (the composition ratio = 90/10, 79/21, 66/34, and 48/52 mol/mol) by anion living polymerization. ESCA analysis of their surface structures (dry state) revealed that PMEA segment was segregated to the top surface in all of the polymers, whereas the results of contact angle of water (wet state) showed that the surfaces were covered with PHEMA segment. In vitro platelet adhesion test showed that these polymers had the excellent compatibility with platelet compared to PHEMA homopolymer. Water structure in the hydrated copolymers was investigated by DSC and freezing bound water was observed for all the polymers like PMEA homopolymer, whereas it was not found in PHEMA homopolymer. Further investigation of water structure based on the results of DSC and EWCMS (equilibrium water content by moisture sorption) suggested that freezing bound water existed in PHEMA segment in addition to PMEA segment. We have proposed that the water plays a key role in the appearance of good blood compatibility of the copolymer, according to our previous works (Tanaka et al. Biomacromolecules 2002;3:36-41, Tanaka et al. J Biomed Mater Res A 2004;68:684-695).

Biocompatible Materials↗
PubMed1987

Immunochemical evidence that the single lactate dehydrogenase of lampreys is more similar to LDHB4 than to LDHA4 of hagfish.

The tetrameric lactate dehydrogenases (LDH) of vertebrates contain several different subunits that arose by gene duplication. While the A and B subunits occur in all classes of gnathostomes, the enzymes of agnathans appear to represent two stages in the evolution of vertebrate LDH. Lampreys of the family Petromyzontidae have a single enzyme classified as LDHA4, while hagfish possess both A and B subunits which form only the two homopolymers LDHA4 and LDHB4. It is generally assumed that the original vertebrate LDH was an A4 type, that duplication to give the B subunit occurred prior to the divergence of lampreys and hagfish, and that modern lampreys subsequently lost expression of the B gene. Lactate dehydrogenases were purified from representatives of all three lamprey families, and it was confirmed that members of the Mordaciidae and Geotriidae also possess single tetrameric LDH enzymes containing one subunit type. The kinetic properties of the lamprey LDH enzymes were compared with the LDH homopolymers of hagfish, skate, and sardine. These properties did not allow the lamprey enzymes to be unequivocally identified as either LDHA4 or LDHB4. Immunochemical titration using antisera against lamprey and hagfish LDH homopolymers demonstrated that the lamprey LDH enzymes showed greater immunochemical similarity to LDHB4 than to LDHA4 of hagfish. It is concluded that there is little evidence for the claim that the original vertebrate LDH was an A4 rather than B4 type.

Animals↗