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Results for “Matrix Bands”

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PubMed2002

A new collagen from the extracellular matrix of Sepia officinalis cartilage.

Guanidinium chloride treatment of Sepia officinalis cartilage solubilized a component that contained hydroxyproline. Electron-microscopy observation of rotary-shadowed preparations of this component revealed it to consist of rod-like units themselves consisting of filaments. Dialysis of an acetic acid solution against ATP afforded polymeric aggregates consisting of a succession of two or three thick sections showing transverse electron-opaque banding, separated by thinner sections without banding. Electrophoresis produced a main band of about 140 kDa sensitive to bacterial collagenase. After reduction with mercaptoethanol, electrophoresis afforded a 40-kDa band. Pepsin digestion resulted in additional electrophoretic bands. These data suggest the presence of a collagen in Sepia cartilage with characteristics unlike those of any known collagen.

Acetic Acid↗

PubMed2005

Proteins of calcified endoskeleton: II partial amino acid sequences of endoskeletal proteins and the characterization of proteinaceous organic matrix of spicules from the alcyonarian, Synularia polydactyla.

Calcified organic substances in the skeleton contain a protein-polysaccharide complex taking a key role in the regulation of bio-calcification. However, information concerning the matrix proteins in alcyonarian and their effect on calcification process is still unknown. For this reason, we have studied the organic matrix of endoskeletal spicules from the alcyonarian coral, Synularia polydactyla, to analyze the proteins with their sequences and investigate the functional properties by a molecular approach. The separated spicules from the colony were identified by scanning electron microscope (SEM). The soluble organic matrix comprised 0.04% of spicule weight. By recording decline of pH in the experimental design, the inhibitory effect of the matrix on CaCO3 precipitation was revealed. Prior to electrophoresis, our analysis of proteins extracted from the soluble organic matrix of the spicules revealed an abundance of proteins in molecular weight. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the preparations showed seven bands of proteins with an apparent molecular mass of 109, 83, 70, 63, 41, 30 and 22 kDa. The proteins were electrophoresed on Tricine-SDS-PAGE after electro-elution treatment, and then transferred to polyvinylidene difluoride (PVDF) membranes and their N-termini were sequenced. Two bands of proteins of about 70 and 63 kDa successfully underwent N-terminal amino acid sequencing. For the detection of calcium binding proteins, a Ca2+ overlay analysis was conducted on the extract by 45Ca autoradiography. The 109 and 63 kDa calcium binding proteins were found to be radioactive. Periodic acid schiff staining indicated that 83 and 63 kDa proteins were glycosylated. An assay for carbonic anhydrase, which is thought to play an important role in the process of calcification revealed low level of the activity. These findings suggest that the endoskeletal spicules of alcyonarian corals have protein-rich organic matrices, which might be related to the calcification process.

Amino Acid Sequence↗

PubMed2005

Role of Au nanoparticles in efficiency enhancement and green band emission quenching of blue polymer light emitting diodes.

We studied photoluminescence (PL) and electroluminescence (EL) properties of polymer light emitting diodes (PLEDs) constructed with polyconjugated polymers blends containing Au nanoparticles (DA-Au NPs; 5.3 nm +/- 1.1 nm in diameter) capped by dodecylamine. For the blue light emitting polyfluorene polymers, selective quenching of excimer peaks or so-called green bands was observed in PL as well as in EL when they were mixed with small amounts (1-4 wt%) of DA-Au NP. The influence of DA-Au NPs on the light-emitting characteristics of the PLEDs strongly depended on the nature of the matrix polymer, which was particularly conspicuous for the polymers whose emission wavelength matches or overlaps with the surface plasmon resonance wavelength region of Au nanoparticles. Especially, the purity of the blue color emitted by the poly [2,7-(9,9-di-n-dioctylfluorene) (PF) was greatly improved by Au NPs that suppressed the 'green band.' All the PLEDs doped with DA-Au NPs showed enhanced maximum external quantum efficiency and emitted light intensity when compared to undoped counterparts.

Amines↗

PubMed1993

Detection of ascorbic acid in the eye of the early chicken embryo by silver staining.

Ascorbate is found in high concentrations in the aqueous, lens and retina of a variety of animal species. Several functions have been proposed for this, including a vital role in aqueous secretion. We investigated the possible presence of ascorbate in the early embryonic chicken eye as a marker for the differentiation of the ciliary epithelium. Embryonic chicken eyes were processed for histochemical demonstration of ascorbate by silver staining. A strongly positive reaction was found in the interstitial matrix between the lens rudiment and the optic vesicle of the 2-day chicken embryo. By 3 days, with lens and optic cup separating from each other, the silver grains were concentrated in the vitreous cavity, primarily in a band-like configuration between the lens equator and the rim of the optic cup, which is the presumptive ciliary epithelium. A weaker reaction was seen in the lens vesicle and primitive neural retina. During the second and third day of incubation the optic vesicle is just beginning to expand. The appearance of ascorbic acid in the newly formed vitreous cavity at this time may indicate its importance in the biosynthesis of the matrix that is filling the expanding optic vesicle.

Animals↗

PubMed1992

The human rhabdomyosarcoma cell line A204 lays down a highly insoluble matrix composed mainly of alpha 1 type-XI and alpha 2 type-V collagen chains.

The biosynthesis of collagen by the A204 cell line was examined using polyclonal antibodies raised against collagen type V and type XI. The study of the pepsin-digested collagen showed that it is composed mainly of alpha 1(XI) and alpha 2(V) collagen chains in an apparent 2:1 ratio, suggesting the formation of heterotypic molecules [alpha 1(XI)]2 alpha 2(V). The existence of this chain stoichiometry was further demonstrated by immunoprecipitation of the molecule with an antibody recognizing alpha 2(V) but not alpha 1(XI) collagen chains. Electron microscopy analyses of 24-h cultures showed that this matrix is composed of thin fibrils, that can be decorated with immunogold-labelled anti-(type-V collagen) IgG, but not with anti-(type-XI collagen) IgG. The collagen matrix laid down by A204 cells is highly insoluble. In the presence of beta-aminopropionitrile, an inhibitor of lysyl oxidase, only a small proportion of intact collagen could be extracted without proteolytic treatment. Immunoblotting of intact medium collagen from cultures performed in the presence of beta-aminopropionitrile showed four distinct bands with each antibody. The migration of the bands, stained with anti-(type-V collagen) IgG, had apparent molecular masses of 127, 149, 161 and 198 kDa (compared to globular standards) while the bands stained with anti-(type-XI collagen) IgG had apparent masses of 145, 182, 207 and 225 kDa. These data indicate that type-V and type-XI collagen chains can assemble in heterotypic isoforms. In this system, the synthesized isoforms are able to aggregate into a highly cohesive matrix and they undergo a proteolytic processing closely similar to that of other fibrillar collagens.

Blotting, Western↗

PubMed2000

Doped rare gas solids as model systems for chromophore-matrix interactions.

Molecular electronic states are extremely sensitive to changes in their environment. Therefore, by inserting probe molecules into a host material and monitoring the ensuing changes in the widths and spectral positions of the electronic absorption bands, interactions of probe and host molecules can be studied. A statistical mechanical model used to analyze these data can also be employed to extract from pressure-induced changes of the band shape information about the local environment of the probe molecule. Dye-doped solid rare gases are ideal model systems to test the basic assumptions of the statistical model, revealing its potential and limitations.

Models, Chemical↗

PubMed1995

Infrared spectroscopy of matrix-isolated polycyclic aromatic hydrocarbon cations. 2. The members of the thermodynamically most favorable series through coronene.

Gaseous, ionized polycyclic aromatic hydrocarbons (PAHs) are thought to be responsible for a very common family of interstellar infrared emission bands. Here the near- and mid-infrared spectra of the cations of the five most thermodynamically favored PAHs up to coronene:phenanthrene, pyrene, benzo[e]pyrene, benzo[ghi]perylene, and coronene, are presented to test this hypothesis. For those molecules that have been studied previously (pyrene, pyrene-d10, and coronene), band positions and relative intensities are in agreement. In all of these cases we report additional features. Absolute integrated absorbance values are given for the phenanthrene, perdeuteriophenanthrene, pyrene, benzo[ghi]perylene, and coronene cations. With the exception of coronene, the cation bands corresponding to the CC modes are typically 2-5 times more intense than those of the CH out-of-plane bending vibrations. For the cations, the CC stretching and CH in-plane bending modes give rise to bands that are an order of magnitude stronger than those of the neutral species, and the CH out-of-plane bends produce bands that are 5-20 times weaker than those of the neutral species. This behavior is similar to that found in most other PAH cations studied to date. The astronomical implications of these PAH cation spectra are also discussed.

Astronomical Phenomena↗

PubMedDate not supplied

Rat heart lipoprotein lipase.

Rat heart lipoprotein lipase was highly purified by affinity chromatography using heparin-Sepharose 4B. When extracts of acetone powder were applied to columns, lipase activity was firmly bound to the gel matrix and was later eluted with 1.5 M NaCl. At this stage the eluted enzyme was purified 1500-fold. Disc gel electrophoresis yielded a single protein band corresponding with the enzyme activity. The apparent molecular weight was 60,000. The purified enzyme was highly unstable; however, its activity could be partially stabilized by glycerol or ethylene glycol. In studying the purified enzyme we observed: (i) a cofactor in serum was required for full enzymatic activity; ApoLp-Glu could be substituted for this cofactor; (ii) ApoLp-Ser was inhibitory to lipase activity; (iii) NaCl and protamine sulfate also markedly inhibited the lipase activity; (iv) heparin stimulated the enzymatic activity.

Animals↗

PubMedDate not supplied

Type Ialpha collagen is an IGFBP-3 binding protein.

Insulin-like growth factor (IGF) binding protein-3 (IGFBP-3) possesses both growth-inhibitory and -potentiating effects on cells, which are independent of IGF action and mediated through specific IGFBP-3 binding proteins/receptors located at the cell membrane, cytosol, or nuclear compartments as well as in the extracellular matrix. We here characterized type Ialpha collagen as one of these IGFBP-3 binding proteins. Human serum was fractionated over an IGFBP-3 affinity column, and bands at 70-100 kDa were eluted as IGFBP-3 ligands. The 100-kDa band was extracted, subjected to N-terminal amino acid sequencing, and identified through database searching as the N-terminal chain of type Ialpha collagen protein. In a separate screening approach, using a yeast two-hybrid system, we cloned the type Ialpha collagen cDNA from a human liver cDNA library as an IGFBP-3 protein partner. Anti-IGFBP-3 antibodies co-immunoprecipitated type Ialpha collagen and IGFBP-3 from the conditioned media of human fibroblasts and vice versa. We demonstrated through ligand dot blot analysis that type Ialpha collagen binds IGFBP-3. IGFBP-3 mutants, with altered sequence at the nuclear localization sequence, bound type Ialpha collagen poorly. Western immunoblot showed that type Ialpha collagen binds only IGFBP-3 but not IGF-I, suggesting an IGF-I-independent mechanism of this interaction. Physiological effects of IGFBP-3-collagen interactions may include modulation of cell adhesion and migration.

Binding Sites↗

PubMed1995

Resonance Raman characterization of H(M200)L mutant reaction centers from Rhodobacter capsulatus. Effects of heterodimer formation on the structural and electronic properties of the cofactors.

Resonance Raman (RR) spectra are reported for photosynthetic reactions centers (RCs) from the H(M200)L mutant of Rhodobacter capsulatus. In this mutant, the histidine residue which ligates the M-side bacteriochlorophyll (BCh) of the special pair primary donor (P) of wild-type RCs is replaced by a noncoordinating leucine. This results in the formation of a heterodimer primary donor (D) in which a bacteriopheophytin (BPh) replaces the M-side BCh. The RR data for the H(M200)L mutant were acquired at a large number of excitation wavelengths which span the B, Qx, and Qy absorption bands of the various bacteriochlorin cofactors in the RC. For comparison, spectra were also acquired for wild-type RCs at the same excitation wavelengths. The RR data obtained for the mutant indicate that heterodimer formation induces a variety of changes in the structural and electronic properties of the cofactors in the RC. These perturbations extend beyond the primary donor and include one of the two accessory BChs. Collectively, the RR studies indicate the following: (1) The structure of the single BCh cofactor in D [DL(BCh)] is different from that of either of the two BChs in P. However, DL(BCh) is more similar to PL than to PM. The PM cofactor is conformationally more distorted than either PL or DL(BCh). (2) The structure of the BPh cofactor in D [DM(BPh)] is similar to that of the other two BPhs in the RC. However, the frequency of the C9-keto carbonyl mode of DM(BPh) is anomalously low (1678 cm-1), as is also the case for PM. The vibrational characteristics of the C9-keto carbonyl vibrations of DM(BPh)/PM versus DL(BCh)/PL are consistent the notion that dielectric effects govern the frequency of the mode and that the effective dielectric constant is different on the L- versus M-sides of the primary donor. (3) Heterodimer formation perturbs the structural and electronic properties of one of the two accessory BChs (most likely BChL) in the RC. These perturbations are manifested as upshifts in the ring skeletal-mode frequencies and a blue-shift in the Qx absorption band (from 600 to 580 nm). The fact that heterodimer formation perturbs one of the accessory BChs suggests that global structural rearrangements occur in the protein matrix when the ligand to a cofactor in the primary donor is removed. (4) For both the H(M200)L mutant and wild-type RCs, oxidation of the primary donor significantly affects the RR cross section of the carotenoid.(ABSTRACT TRUNCATED AT 400 WORDS)

Bacteriochlorophylls↗

PubMed2005

Characterization and quantification of proteins in lecithins.

Several methods for extraction and quantification of proteins from lecithins were compared. Extraction with hexane-2-propanol-water followed by amino acid analysis is the most suitable method for isolation and quantification of proteins from lecithins. The detection limit of the method is 15 mg protein/kg lecithin, and the quantification limit is 50 mg protein/kg. The relative repeatability limits for samples containing 0-500 and 500-5000 mg protein/kg sample were 12.6 and 7.5%, respectively. The protein recovery ranged between 101 and 123%. The protein content has been determined in different kinds of lecithins. The results were as follows: standard soy lecithins (between 232 and 1338 mg/kg), deoiled soy lecithin (342 mg/kg), phosphatydylcholine-enriched soy lecithins (not detectable and 163 mg/kg), sunflower lecithins (892 and 414 mg/kg), and egg lecithin (50 mg/kg). The sodium dodecyl sulfate-polyacrylamide gel electrophoresis protein patterns of the standard soy and sunflower lecithins are very similar to those of soy flour. The protein profile of the egg lecithin shows several bands with a broad range of molecular masses. The molecular masses of the main proteins of soy lecithins and soy flour have been determined by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) and ranged from 10.5 to 52.2 kDa. Most of the major proteins from soy and sunflower lecithins identified by MALDI-MS and electrospray tandem MS belong to the 11S globulin fraction, which is one of the main fractions of soy and sunflower seeds. In addition, the seed maturation protein P34 from the 7S globulin fraction of soy proteins has also been identified in soy lecithins. This protein has been reported as the most allergenic protein in soybean.

Amino Acids↗

PubMed1998

cDNA cloning of Batis maritima methyl chloride transferase and purification of the enzyme.

Methyl chloride transferase catalyzes the synthesis of methyl chloride from S-adenosine-L-methionine and chloride ion. This enzyme has been purified 2,700-fold to homogeneity from Batis maritima, a halophytic plant that grows abundantly in salt marshes. The purification of the enzyme was accomplished by a combination of ammonium sulfate fractionation, column chromatography on Sephadex G100 and adenosine-agarose, and TSK-250 size-exclusion HPLC. The purified enzyme exhibits a single band on SDS/PAGE with a molecular mass of approximately 22.5 kDa. The molecular mass of the purified enzyme was 22,474 Da as determined by matrix-associated laser desorption ionization mass spectrometry. The methylase can function in either a monomeric or oligomeric form. A 32-aa sequence of an internal fragment of the methylase was determined (GLVPGCGGGYDVVAMANPER FMVGLDIXENAL, where X represents unknown residue) by Edman degradation, and a full-length cDNA of the enzyme was obtained by rapid amplification of cDNA ends-PCR amplification of cDNA oligonucleotides. The cDNA gene contains an ORF of 690 bp encoding an enzyme of 230 aa residues having a predicted molecular mass of 25,761 Da. The disparity between the observed and calculated molecular mass suggests that the methylase undergoes posttranslational cleavage, possibly during purification. Sequence homologies suggest that the B. maritima methylase defines a new family of plant methyl transferases. A possible function for this novel methylase in halophytic plants is discussed.

Amino Acid Sequence↗

PubMed2002

Purification of turnip peroxidase and its kinetic properties.

Peroxidase from turnip roots was purified using metal affinity chromatography up to a specific activity of 337 units/mg protein with 3.02 RZ and 63.5% recovery. After purification, the enzyme showed 2-3 bands on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight of the purified enzyme was found to be 37-39 kD with matrix assisted laser desorption ionization mass spectrometer (MALDI-MS). The enzyme showed maximum activity in phosphate buffer, pH 6.0, and lowest activity in borate buffer at the same pH. The Km of the enzyme was found to be 7.07 x 104 mM. Turnip peroxidase also contains an iron moiety which is found to be about 0.28%. The enzyme showed 50% inhibition of its specific activity with ethylene diamine tetraacetic acid (EDTA).

Brassica napus↗

PubMed1993

Human dystroglycan: skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization.

Dystroglycan is a novel laminin binding component of the dystrophin-glycoprotein complex which provides a linkage between the subsarcolemmal cytoskeleton and the extracellular matrix. Here we report the cDNA and genomic structure of human dystroglycan. The human dystroglycan is encoded by a single gene (DAG1) mapped to chromosome 3 band p21. The coding sequence is organized into two exons, separated by a large intron. The predicted amino acid sequence of human and rabbit dystroglycan are 93% identical with predicted glycosylation sites being conserved. Human dystroglycan is expressed in a variety of fetal and adult tissues. Our data suggest that muscle and non-muscle isoforms of dystroglycan differ by carbohydrate moieties but not protein sequence. Therefore, we hypothesize that variable glycosylation of the conserved protein core might modulate laminin binding. The relationship of dystroglycan to human diseases is discussed.

Amino Acid Sequence↗

PubMed2006

Energy dispersion of 4f-derived emissions in photoelectron spectra of the heavy-fermion compound YbIr2Si2.

Angle-resolved photoemission spectra of the heavy-fermion system YbIr(2)Si(2) are reported that reveal strong momentum (k) dependent splittings of the 4f(13) bulk and surface emissions around the expected intersection points of the 4f final states with valence bands in the Brillouin zone. The obtained dispersion is explained in terms of a simplified periodic Anderson model by a k dependence of the electron hopping matrix element disregarding clearly interpretation in terms of a single-impurity model.

Journal Article↗

PubMed1996

The effects of CO2 laser and Nd:YAG with and without water/air surface cooling on tooth root structure: correlation between FTIR spectroscopy and histology.

Morphologic and chemical characterization of root surfaces treated with either the CO2 laser, Nd:YAG, or Nd:YAG with water/air surface cooling (Nd:YAG-C) was completed using scanning electron microscopy (SEM) and FTIR photoacoustic spectroscopy (FTIR/PAS). Specimens for morphologic analysis consisted of 20 extracted single rooted teeth unaffected by periodontal disease. The specimens were exposed at varying energy densities to a single pass of the laser. SEM examination revealed, for all lasers, a direct correlation between increasing energy densities and depth of tissue ablation and width of tissue damage. The Nd:YAG-C required higher energy densities than either the CO2 or Nd:YAG lasers to achieve the same relative depth of tissue ablation. Regardless of energy density, and in contrast with other laser types, areas treated with the Nd:YAG-C did not exhibit collateral zones of heat damage. Specimens for spectroscopic examination consisted of 12 disks, 6 x 2 mm, cut from debrided root surfaces of extracted, unerupted human molars. The spectral results indicate a substantial reduction in the absorption bands attributable to protein and an additional band at 2015 cm-1 in specimens exposed to the Nd:YAG without water. In the presence of water/air coolant, the band at 2015 cm-1 appears only at a substanially higher energy density. The spectra of the CO2 treated specimens, with the char layer present, show a significant reduction in the protein bands and additional bands at 2015 and 2200 cm-1, that are tentatively assigned to the cyanamide and cyanate ions, respectively. These results suggest a reaction of the organic matrix and mineral with laser exposure.

Acoustics↗

PubMed2003

Examination of the factor structure of center of foot pressure movement and cross-validity.

This study aimed to determine the factor structure of the center of foot pressure (CFP) movement during static upright posture, and to objectively categorize and summarize parameters to evaluate CFP movement. The subjects were 220 healthy young males and females. The measurement of CFP was carried out 3 times with 1 min rest and the mean of trials 2 and 3 was used for the analysis. The measurement device was an Anima's stabilometer G5500. The data sampling frequency was 20 Hz. Thirty-four parameters with high reliability were selected from the following 6 domains except for the center position which is a fundamental attribute: distance, distribution of amplitude, area, velocity, power spectrum, and body sway vector. Factor analysis (principal factor method and promax rotation) was applied to a correlation matrix consisting of 32 parameters. Four factors abstracted were interpreted as follows; unit time sway, front and back sway, left and right sway and high frequency band of power spectrum. The reliability coefficient (ICC=0.89-0.95) and the congruence coefficient (phi=0.80-0.97) between factors abstracted from the original and the cross-validity groups were very high. It was considered that the CFP movement consists of the above 4 factors that evaluate the amount of body sway and can be synthetically evaluated by them.

Biomechanical Phenomena↗

PubMedDate not supplied

Childhood longitudinal melanonychia: case reports and review of the literature.

"Longitudinal melanonychia" refers to a brown or brown-black longitudinal band on a fingernail or toenail. A number of conditions can cause longitudinal melanonychia, but its main importance is that, in some patients, it may indicate the presence of a subungual malignant melanoma. Hyperpigmented nail bands are not uncommon in African-American, Latino and Asian patients, especially those over sixty years of age, and are often multiple in these groups. Longitudinal melanonychia is most worrisome when there is a solitary, dark, broad longitudinal band with pigment extending over the proximal nail fold (Hutchinson's sign). Such findings are considered to be a strong indication for biopsy of the nail matrix to rule out melanoma. Since nail matrix biopsy sometimes results in permanent nail deformity, and since the incidence of malignant melanoma is quite small in the pediatric age group, there is some controversy as to whether this procedure should routinely be performed in children. We report two cases of dramatic longitudinal melanonychia in toddlers and review the current literature on the management of this striking condition in the pediatric age group.

Adolescent↗