Base de dados : MEDLINE
Pesquisa : D12.776.660.750.270 [Categoria DeCS]
Referências encontradas : 37 [refinar]
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[PMID]:11428574
[Au] Autor:Hansen LT; Austin JW; Gill TA
[Ad] Endereço:Canadian Institute of Fisheries Technology, Dalhousie University, Halifax, Nova Scotia. ltruelst@is.dal.ca
[Ti] Título:Antibacterial effect of protamine in combination with EDTA and refrigeration.
[So] Source:Int J Food Microbiol;66(3):149-61, 2001 Jun 15.
[Is] ISSN:0168-1605
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The antimicrobial effect of protamine (clupeine) on a range of gram-positive and gram-negative foodborne pathogens and spoilage bacteria, was evaluated using an agar dilution assay and a broth dilution assay with Alamar Blue as growth indicator. Protamine was tested alone at concentrations from 0 to 10,000 microg/ml, and in combination with EDTA (0.9 mM). Assays were performed at 5 degrees C, 10 degrees C, 18 degrees C and 30 degrees C to test the effect of temperature. Minimum inhibitory concentration (MIC) values ranged from 10 microg/ml for Brochothrix thermosphacta to no inhibition at 10,000 microg/ml for bacteria such as Aeromonas hydrophila, proteolytic strains of Clostridium botulinum, Hafnia alvei and Morganella morganii. The minimum bactericidal concentrations (MBCs) were generally higher than MICs. In combination with EDTA, MICs of protamine decreased for gram-negative test strains, whereas EDTA alone inhibited gram-positive strains. The effect of assay incubation temperature was variable and not clear for most strains. Concentrations of 100-750 microg/ml protamine inhibited the five non-proteolytic C. botulinum strains, while none of the eight proteolytic strains was inhibited, indicating the possible role of proteolytic enzymes in protecting cells from protamine. Clearing zones, indicative of proteolytic activity, were observed in the opaque TSB-agarose around colonies of some but not all protamine-resistant bacteria, suggesting that this is not the only resistance mechanism. Addition of 5% (w/v) gelatin to study the effect of an increased protein concentration in the agar dilution assay showed that electrostatic interactions between protamine and the protein decreased the antimicrobial efficacy of the peptide.
[Mh] Termos MeSH primário: Clupeína/farmacologia
Ácido Edético/farmacologia
Aditivos Alimentares/farmacologia
Bactérias Gram-Negativas/efeitos dos fármacos
Bactérias Gram-Positivas/efeitos dos fármacos
[Mh] Termos MeSH secundário: Contagem de Colônia Microbiana
Combinação de Medicamentos
Conservantes de Alimentos/farmacologia
Gelatina/farmacologia
Bactérias Gram-Negativas/crescimento & desenvolvimento
Bactérias Gram-Positivas/crescimento & desenvolvimento
Testes de Sensibilidade Microbiana
Peptídeo Hidrolases/metabolismo
Refrigeração
Temperatura Ambiente
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Drug Combinations); 0 (Food Additives); 0 (Food Preservatives); 9000-70-8 (Gelatin); 9007-31-2 (Clupeine); 9G34HU7RV0 (Edetic Acid); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:0107
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:010629
[St] Status:MEDLINE


  2 / 37 MEDLINE  
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[PMID]:8743574
[Au] Autor:Kumon A; Kodama H; Kondo M; Yokoi F; Hiraishi H
[Ad] Endereço:Department of Biochemistry, Saga Medical School.
[Ti] Título:N(omega)-phosphoarginine phosphatase (17 kDa) and alkaline phosphatase as protein arginine phosphatases.
[So] Source:J Biochem;119(4):719-24, 1996 Apr.
[Is] ISSN:0021-924X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Seven synthetic polymers, (Glu4, Tyr)n, (Arg)n, (Arg, Pro, Thr)n, (Arg-Gly-Glu)6, (Arg-Gly-Phe)6, (Glu-Arg-Gly-Phe)5, and (Ala-Leu-Arg-Arg-Ile-Arg-Gly-Glu-Arg)2, were treated with phosphoryl chloride to phosphorylate their Tyr, Thr, and Arg residues. Protamines and histones were phosphorylated similarly. These phosphorylated peptides were examined as to whether or not they serve as substrates for intestinal alkaline phosphatase [EC 3.1.3.1] and liver N(omega)-phosphoarginine phosphatase [Kuba, M., Ohmori, H., and Kumon, A. (1992) Eur. J. Biochem. 208, 747-752]. Phosphorylated polyarginine was hydrolyzed with a lower Km with alkaline phosphatase than with N(omega)-phosphoarginine phosphatase, while the phosphorylated forms of (Arg-Gly-Phe)6 and culpeine were better substrates for N(omega)-phosphoarginine phosphatase. When (Arg, Pro, Thr)n and culpeine were phosphorylated chemically after treatment with phenylglyoxal, these phosphorylated peptides were worse substrates for N(omega)-phosphoarginine phosphatase than for alkaline phosphatase. Moreover, the results of proton-decoupled 31P NMR analysis indicated that N(omega)-phosphoarginine phosphatase released Pi from N(omega)-phosphoarginine residues of phosphopeptides. These results indicate that both phosphatases function as protein arginine phosphatases in different manners, and that N(omega)-phosphoarginine phosphatase is useful for selectively detecting N(omega)-phosphoarginine residue in peptides containing various kinds of phosphorylated amino acids.
[Mh] Termos MeSH primário: Fosfatase Alcalina/metabolismo
Arginina/análogos & derivados
Hidrolases/metabolismo
Compostos de Fósforo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Arginina/análise
Arginina/metabolismo
Bovinos
Clupeína/metabolismo
Histonas/química
Hidrólise
Intestinos/enzimologia
Cinética
Fígado/enzimologia
Dados de Sequência Molecular
Oligopeptídeos/síntese química
Oligopeptídeos/metabolismo
Compostos Organofosforados/análise
Compostos Organofosforados/metabolismo
Fosfatos/análise
Fosfopeptídeos/síntese química
Fosfopeptídeos/metabolismo
Fósforo
Fosfotirosina/análise
Ratos
Salmina/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Histones); 0 (Oligopeptides); 0 (Organophosphorus Compounds); 0 (Phosphates); 0 (Phosphopeptides); 0 (Phosphorus Compounds); 1189-11-3 (phospho-L-arginine); 21820-51-9 (Phosphotyrosine); 27YLU75U4W (Phosphorus); 9007-31-2 (Clupeine); 9014-82-8 (Salmine); 94ZLA3W45F (Arginine); 9XM78OL22K (phosphoryl chloride); EC 3.- (Hydrolases); EC 3.1.3.1 (Alkaline Phosphatase); EC 3.9.1.- (N-omega-phosphoarginine hydrolase)
[Em] Mês de entrada:9610
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:960401
[St] Status:MEDLINE


  3 / 37 MEDLINE  
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Fotocópia
[PMID]:7668395
[Au] Autor:Nedved ML; Moe GR
[Ad] Endereço:Department of Chemistry and Biochemistry, University of Delaware, Newark 19716, USA.
[Ti] Título:The use of affinity coelectrophoresis to characterize cooperative, nonspecific nucleic acid binding peptides.
[So] Source:Anal Biochem;227(1):80-4, 1995 May 01.
[Is] ISSN:0003-2697
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Affinity coelectrophoresis (ACE) is a technique for characterizing ligand/nucleic acid binding interactions under equilibrium conditions. It is used here to characterize the protamine clupeine Z binding to several DNA fragments in order to define the use and limitations of ACE for ligands that bind cooperatively and nonspecifically to nucleic acids. The results demonstrate that the ACE data for cooperative, nonspecific ligands can be analyzed using the McGhee-von Hippel model and that binding-site sizes can be accurately determined using lattices containing as few as one site. However, binding constants can be greatly underestimated for some cooperative ligands with large-site sizes if small lattices are used. The salt dependence of the binding constant can also be determined but is limited to salt concentrations less than approximately 300 mM. Given the simplicity and reproducibility of the ACE assay, it should find many applications for studying binding interactions for a variety of cooperative and noncooperative nucleic acid binding peptides and proteins.
[Mh] Termos MeSH primário: Clupeína/metabolismo
Proteínas de Ligação a DNA/metabolismo
DNA/metabolismo
Eletroforese em Gel de Ágar/métodos
Peptídeos/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
DNA/genética
Proteínas de Ligação a DNA/química
Cinética
Peptídeos/química
Ligação Proteica
Cloreto de Sódio/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Peptides); 451W47IQ8X (Sodium Chloride); 9007-31-2 (Clupeine); 9007-49-2 (DNA)
[Em] Mês de entrada:9510
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:950501
[St] Status:MEDLINE


  4 / 37 MEDLINE  
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Fotocópia
[PMID]:8448186
[Au] Autor:D'Auria G; Paolillo L; Sartorio R; Wurzburger S
[Ad] Endereço:Department of Chemistry, University Federico II, Naples, Italy.
[Ti] Título:Structure and function of protamines: an 1H nuclear magnetic resonance investigation of the interaction of clupeines with mononucleotides.
[So] Source:Biochim Biophys Acta;1162(1-2):209-16, 1993 Mar 05.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Protamines form a class of low-molecular-weight proteins that protect the chromosomal DNA in the spermatic cells of eukaryotic organisms. Protamines are located in the small and/or large groove of DNA where they complex the DNA nucleotides. Very little is known up to date on the role and specificity of binding of the various protamine fractions belonging to a single eukaryotic species. In the present paper, a detailed investigation on the complexation properties of the protamine fractions (clupeines) extracted from herrings has been carried out by means of proton nuclear magnetic resonance and ultraviolet absorbtion data. In particular, the binding properties of the clupeine fractions with purinic (5'dAMP) and pyrimidinic (5'dCMP) mononucleotides have been measured and analysed at different clupeine concentrations. The results indicate that, contrary to previous preliminary hypothesis, the three clupeine fractions exhibit quite comparable binding properties toward mononucleotides. In addition it has been found that nucleotides can induce a conformational transition of the disorder-order type in the clupeine molecules and this property is concentration and temperature dependent. It is concluded that, as far as specificity is concerned, the clupeine fractions seem to possess the same behaviour toward mononucleotides.
[Mh] Termos MeSH primário: Clupeína/química
Nucleotídeos/química
Protaminas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Clupeína/metabolismo
Espectroscopia de Ressonância Magnética
Dados de Sequência Molecular
Nucleotídeos/metabolismo
Espectrofotometria Ultravioleta
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nucleotides); 0 (Protamines); 9007-31-2 (Clupeine)
[Em] Mês de entrada:9304
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:930305
[St] Status:MEDLINE


  5 / 37 MEDLINE  
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Fotocópia
[PMID]:1426617
[Au] Autor:Kuhn NJ; Stankiewicz M; Ward S
[Ad] Endereço:School of Biochemistry, University of Birmingham, U.K.
[Ti] Título:Cation activation and stabilization of Golgi beta 1,4-galactosyltransferase (lactose synthetase).
[So] Source:Biochem Soc Trans;20(3):714-6, 1992 Aug.
[Is] ISSN:0300-5127
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Complexo de Golgi/enzimologia
Lactose Sintase/metabolismo
Manganês/farmacologia
[Mh] Termos MeSH secundário: Animais
Cálcio/farmacologia
Cátions Bivalentes
Clupeína/farmacologia
Ativação Enzimática
Estabilidade Enzimática
Cinética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Cations, Divalent); 42Z2K6ZL8P (Manganese); 9007-31-2 (Clupeine); EC 2.4.1.22 (Lactose Synthase); SY7Q814VUP (Calcium)
[Em] Mês de entrada:9212
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:920801
[St] Status:MEDLINE


  6 / 37 MEDLINE  
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Fotocópia
[PMID]:1960734
[Au] Autor:Porschke D
[Ad] Endereço:Max Planck Institut für biophysikalische Chemie, Göttingen, Germany.
[Ti] Título:Nature of protamine-DNA complexes. A special type of ligand binding co-operativity.
[So] Source:J Mol Biol;222(2):423-33, 1991 Nov 20.
[Is] ISSN:0022-2836
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The mode of protamine binding to DNA double helices has been analyzed for the example of clupein Z from herring and DNA samples from bacteriophages lambda and PM2 by measurements of light-scattering intensities, ultracentrifugation and kinetics. The light-scattering intensity of DNA increases co-operatively at a threshold clupein concentration suggesting co-operative binding of clupein to double helices. These data are first analyzed in terms of a model with a transition at a threshold degree of binding. The parameters resulting from this analysis appear to be reasonable, but are shown to be in contrast with data on the absolute degree of clupein binding to DNA obtained by centrifugation experiments. An analysis of the kinetics associated with clupein binding to DNA by measurements of the time-dependence of light-scattering intensities in the time range of seconds demonstrates directly that clupein-induced intermolecular interactions of DNA molecules are essential. The rate constants of DNA association increase co-operatively at threshold clupein concentrations, which correspond to those observed in the equilibrium titrations. Above the threshold, the rate constants arrive at a level that is almost constant, but shows some decrease with increasing clupein concentrations. These results are described by a model with a monomer and a dimer state of DNA, which bind ligands with different affinities according to an excluded-site binding scheme. When the ligand binding constant is larger for the dimer than for the monomer state, as should be expected, binding of ligands drives the DNA from the monomer to the dimer state, even if the dimerization equilibrium in the absence of ligands is far in favor of the monomer. The transition from the monomer to the dimer state proves to be strongly co-operative. When the ligand concentration is increased to higher values, the dimers may be converted back to monomers due to an increased extent of ligand binding to the monomer state. The model is consistent with the available experimental data. The analysis of the data by the model indicates the existence of a reaction unit much below the DNA chain length, corresponding to about 80 nucleotide residues. The present model describes ligand driven intermolecular association; an analogous model is applicable to ligand driven intramolecular association. In summary, the co-operativity of clupein binding to DNA double helices is not due to nearest neighbor interactions, but results from thermodynamic coupling of clupein binding with clupein-induced DNA association.
[Mh] Termos MeSH primário: Clupeína/química
DNA Viral/química
Protaminas/química
[Mh] Termos MeSH secundário: Bacteriófagos/química
Centrifugação
Técnicas In Vitro
Ligantes
Luz
Espalhamento de Radiação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral); 0 (Ligands); 0 (Protamines); 9007-31-2 (Clupeine)
[Em] Mês de entrada:9201
[Cu] Atualização por classe:141120
[Lr] Data última revisão:
141120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:911120
[St] Status:MEDLINE


  7 / 37 MEDLINE  
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Fotocópia
[PMID]:1917295
[Au] Autor:Ishimura M; Nishi N; Uedaira H
[Ad] Endereço:Research Institute for Polymers and Textiles, Ibaraki, Japan.
[Ti] Título:Hydration of clupeine in solution.
[So] Source:Int J Pept Protein Res;37(5):399-401, 1991 May.
[Is] ISSN:0367-8377
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:Spin-lattice relaxation times, T1, of H2(17) O at 25 degrees were measured for aqueous solutions of clupeine and its constituent amino acids, which are serine, threonine, proline and arginine. The dynamic hydration numbers, nDHN, of clupeine and amino acids were determined from a concentration dependence of T1. The coordination numbers nh, and the rotational correlation times, tau ch, of water molecules around clupeine and amino acids were estimated and compared with that of pure water. The tau ch/tau co of clupeine was 1.85 and close to that of arginine. The experimental value of nDHN of clupeine was in good agreement with that calculated from the nDHN values of the constituent amino acids. This means that the clupeine molecule has a random conformation in solution.
[Mh] Termos MeSH primário: Clupeína/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Aminoácidos/química
Espectroscopia de Ressonância Magnética/métodos
Dados de Sequência Molecular
Soluções
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Solutions); 9007-31-2 (Clupeine)
[Em] Mês de entrada:9110
[Cu] Atualização por classe:001218
[Lr] Data última revisão:
001218
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:910501
[St] Status:MEDLINE


  8 / 37 MEDLINE  
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Fotocópia
[PMID]:1772633
[Au] Autor:Balschmidt P; Hansen FB; Dodson EJ; Dodson GG; Korber F
[Ad] Endereço:Novo-Nordisk A/S, Gentofte, Denmark.
[Ti] Título:Structure of porcine insulin cocrystallized with clupeine Z.
[So] Source:Acta Crystallogr B;47 ( Pt 6):975-86, 1991 Dec 01.
[Is] ISSN:0108-7681
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The crystal structure of NPH-insulin, pig insulin cocrystallized with zinc, m-cresol and protamine, has been solved by molecular replacement and refined using restrained least-squares refinement methods. The final crystallographic R factor for all reflections between 2 and 10 A is 19.4%. The insulin molecules are arranged as hexamers with two tetrahedrally coordinated Zn atoms in the central channel and one m-cresol bound to each monomer near His B5. One protamine binding site has been unequivocally identified near a dimer-dimer interface, although most of the polypeptide is crystallographically disordered. The conformation of the insulin moiety and the structural differences between the three unique monomers have been analysed. The zinc and m-cresol environments are described and the nature of the protamine binding site is outlined.
[Mh] Termos MeSH primário: Clupeína/metabolismo
Insulina/metabolismo
[Mh] Termos MeSH secundário: Animais
Cresóis/metabolismo
Cristalização
Estrutura Molecular
Protaminas/metabolismo
Conformação Proteica
Suínos
Difração de Raios X
Zinco/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cresols); 0 (Insulin); 0 (Protamines); 9007-31-2 (Clupeine); GGO4Y809LO (3-cresol); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:9202
[Cu] Atualização por classe:161123
[Lr] Data última revisão:
161123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:911201
[St] Status:MEDLINE


  9 / 37 MEDLINE  
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Fotocópia
[PMID]:1698194
[Au] Autor:Saiki I; Murata J; Makabe T; Nishi N; Tokura S; Azuma I
[Ad] Endereço:Institute of Immunological Science, Hokkaido University, Sapporo.
[Ti] Título:Inhibition of tumor angiogenesis by a synthetic cell-adhesive polypeptide containing the Arg-Gly-Asp (RGD) sequence of fibronectin, poly(RGD).
[So] Source:Jpn J Cancer Res;81(6-7):668-75, 1990 Jun-Jul.
[Is] ISSN:0910-5050
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:We have investigated the anti-angiogenic effect of a polymeric peptide based on the Arg-Gly-Asp (RGD) core sequence of fibronectin as a monomer unit, i.e., poly(RGD), in syngeneic mice and in vitro. Single intratumoral administration of poly(RGD) on day 0, 1 or 7 after tumor implantation achieved a significant reduction of B16-BL6 melanoma colonization in the lungs, but did not affect the size of the primary tumor at the time of amputation. The number of capillary blood vessels oriented toward the tumor mass increased during the early growth phase after the intradermal inoculation of the tumor. Poly(RGD) significantly inhibited the formation of tumor neovascularization when co-injected with the tumor cells or separately injected intratumorally or intravenously on day 1 or 3 after tumor inoculation. This inhibitory effect of poly(RGD) was dose-dependent. Poly(RGD) was able to inhibit the haptotactic migration of endothelial cells along a gradient of substratum-immobilized fibronectin but not laminin. Tumor-conditioned medium (CM) by itself did not act as a chemoattractant when it was added in the lower compartment of a Transwell chamber, but promoted the endothelial cell migration to immobilized fibronectin or laminin. Poly(RGD) inhibited the enhanced cell migration to fibronectin but not to laminin in response to CM. Thus, poly(RGD)-mediated inhibition of tumor metastasis may be partly due to the inhibition of tumor-induced angiogenesis at primary and secondary sites.
[Mh] Termos MeSH primário: Fibronectinas/farmacologia
Neoplasias Pulmonares/irrigação sanguínea
Neovascularização Patológica
Oligopeptídeos/farmacologia
Peptídeos/farmacologia
[Mh] Termos MeSH secundário: Animais
Movimento Celular/efeitos dos fármacos
Clupeína/farmacologia
Relação Dose-Resposta a Droga
Técnicas In Vitro
Injeções Intradérmicas
Laminina/farmacologia
Neoplasias Pulmonares/tratamento farmacológico
Neoplasias Pulmonares/secundário
Camundongos
Camundongos Endogâmicos C57BL
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fibronectins); 0 (Laminin); 0 (Oligopeptides); 0 (Peptides); 119865-10-0 (poly (arginyl-glycyl-aspartic acid)); 78VO7F77PN (arginyl-glycyl-aspartic acid); 9007-31-2 (Clupeine)
[Em] Mês de entrada:9010
[Cu] Atualização por classe:161123
[Lr] Data última revisão:
161123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:900601
[St] Status:MEDLINE


  10 / 37 MEDLINE  
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[PMID]:2755968
[Au] Autor:Bonincontro A; Caneva R; Pedone F; Romano TF
[Ad] Endereço:Dipartimento di Fisica, GNSM-CISM, Universitá La Sapienza, Roma, Italy.
[Ti] Título:Complex dielectric constant of arginine-DNA and protamine-DNA aqueous systems at 10 GHz.
[So] Source:Phys Med Biol;34(5):609-16, 1989 May.
[Is] ISSN:0031-9155
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The complex dielectric constant of arginine and protamine from herring sperm (clupeine) and their complexes with herring sperm DNA was measured at 10 GHz in the temperature range -20 to +45 degrees C by a microwave cavity perturbation method. The experimental results were analysed in terms of a three-component equation (solute molecules, interfacial water and bulk water) to calculate the fractional volume of modified water and hence the specific hydration of the samples. A fourfold reduction of the specific hydration is observed for the clupeine molecule as compared to the free monomers. This is consistent with a folded conformation of the protein in solution. The specific hydration of the complex between clupeine and DNA is reduced by 50% with respect to the weighted average for the uncomplexed components. This result indicates an intimate contact between clupeine and DNA with exclusion of water molecules and is consistent with the highly condensed form of nucleoprotamines which is known in vivo.
[Mh] Termos MeSH primário: Arginina
DNA
Protaminas
Espermatozoides/análise
[Mh] Termos MeSH secundário: Animais
Clupeína
Condutividade Elétrica
Peixes
Técnicas In Vitro
Masculino
Água
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protamines); 0 (deoxyribonucleoprotamine); 059QF0KO0R (Water); 9007-31-2 (Clupeine); 9007-49-2 (DNA); 94ZLA3W45F (Arginine)
[Em] Mês de entrada:8908
[Cu] Atualização por classe:141120
[Lr] Data última revisão:
141120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:890501
[St] Status:MEDLINE



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