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[PMID]:27288155
[Au] Autor:Lepeshkevich SV; Gilevich SN; Parkhats MV; Dzhagarov BM
[Ad] Endereço:B.I. Stepanov Institute of Physics, National Academy of Sciences of Belarus, 68 Nezavisimosti Ave, Minsk 220072, Belarus. Electronic address: lepeshkevich@imaph.bas-net.by.
[Ti] Título:Molecular oxygen migration through the xenon docking sites of human hemoglobin in the R-state.
[So] Source:Biochim Biophys Acta;1864(9):1110-1121, 2016 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A nanosecond laser flash-photolysis technique was used to study bimolecular and geminate molecular oxygen (O2) rebinding to tetrameric human hemoglobin and its isolated α and ß chains in buffer solutions equilibrated with 1atm of air and up to 25atm of xenon. Xenon binding to the isolated α chains and to the α subunits within tetrameric hemoglobin was found to cause a decrease in the efficiency of O2 escape by a factor of ~1.30 and 3.3, respectively. A kinetic model for O2 dissociation, rebinding, and migration through two alternative pathways in the hemoglobin subunits was introduced and discussed. It was shown that, in the isolated α chains and α subunits within tetrameric hemoglobin, nearly one- and two-third escaping molecules of O2 leave the protein via xenon docking sites, respectively. The present experimental data support the idea that O2 molecule escapes from the ß subunits mainly through the His(E7) gate, and show unambiguously that, in the α subunits, in addition to the direct E7 channel, there is at least one alternative escape route leading to the exterior via the xenon docking sites.
[Mh] Termos MeSH primário: Hemoglobinas/química
Oxigênio/química
Subunidades Proteicas/química
Xenônio/química
[Mh] Termos MeSH secundário: Ditiotreitol/química
Hemoglobinas/isolamento & purificação
Seres Humanos
Cinética
Mercurobenzoatos/química
Simulação de Acoplamento Molecular
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Estrutura Secundária de Proteína
Subunidades Proteicas/isolamento & purificação
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-mercuribenzoate); 0 (Hemoglobins); 0 (Mercuribenzoates); 0 (Protein Subunits); 3H3U766W84 (Xenon); S88TT14065 (Oxygen); T8ID5YZU6Y (Dithiothreitol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160612
[St] Status:MEDLINE


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[PMID]:23600730
[Au] Autor:Smith CA; Simpson CA; Kim G; Carter CJ; Feldheim DL
[Ad] Endereço:Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309, United States.
[Ti] Título:Gastrointestinal bioavailability of 2.0 nm diameter gold nanoparticles.
[So] Source:ACS Nano;7(5):3991-6, 2013 May 28.
[Is] ISSN:1936-086X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The use of gold nanoparticles as imaging agents and therapeutic delivery systems is growing rapidly. However, a significant limitation of gold nanoparticles currently is their low absorption efficiencies in the gastrointestinal (GI) tract following oral administration. In an attempt to identify ligands that facilitate gold nanoparticle absorption in the GI tract, we have studied the oral bioavailability of 2.0 nm diameter gold nanoparticles modified with the small molecules p-mercaptobenzoic acid and glutathione, and polyethylene glycols (PEG) of different lengths and charge (neutral and anionic). We show that GI absorption of gold nanoparticles modified with the small molecules tested was undetectable. However, the absorption of PEGs depended upon PEG length, with the shortest PEG studied yielding gold nanoparticle absorptions that are orders-of-magnitude larger than observed previously. As the oral route is the most convenient one for administering drugs and diagnostic reagents, these results suggest that short-chain PEGs may be useful in the design of gold nanoparticles for the diagnosis and treatment of disease.
[Mh] Termos MeSH primário: Trato Gastrointestinal/metabolismo
Ouro/química
Ouro/farmacocinética
Nanopartículas Metálicas
Tamanho da Partícula
[Mh] Termos MeSH secundário: Animais
Disponibilidade Biológica
Feminino
Glutationa/química
Mercurobenzoatos/química
Camundongos
Camundongos Endogâmicos BALB C
Modelos Moleculares
Conformação Molecular
Polietilenoglicóis/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (4-mercuribenzoate); 0 (Mercuribenzoates); 30IQX730WE (Polyethylene Glycols); 7440-57-5 (Gold); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1310
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130423
[St] Status:MEDLINE
[do] DOI:10.1021/nn305930e


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[PMID]:11969426
[Au] Autor:Chang CK; Simplaceanu V; Ho C
[Ad] Endereço:Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.
[Ti] Título:Effects of amino acid substitutions at beta 131 on the structure and properties of hemoglobin: evidence for communication between alpha 1 beta 1- and alpha 1 beta 2-subunit interfaces.
[So] Source:Biochemistry;41(17):5644-55, 2002 Apr 30.
[Is] ISSN:0006-2960
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Substitutions of Asn, Glu, and Leu for Gln at the beta131 position of the hemoglobin molecule result in recombinant hemoglobins (rHbs) with moderately lowered oxygen affinity and high cooperativity compared to human normal adult hemoglobin (Hb A). The mutation site affects the hydrogen bonds present at the alpha(1)beta(1)-subunit interface between alpha103His and beta131Gln as well as that between alpha122His and beta35Tyr. NMR spectroscopy shows that the hydrogen bonds are indeed perturbed; in the case of rHb (beta131Gln --> Asn) and rHb (beta131Gln --> Leu), the perturbations are propagated to the other alpha(1)beta(1)-interface H-bond involving alpha122His and beta35Tyr. Proton exchange measurements also detect faster exchange rates for both alpha(1)beta(1)-interface histidine side chains of the mutant rHbs in 0.1 M sodium phosphate buffer at pH 7.0 than for those of Hb A under the same conditions. In addition, the same measurements in 0.1 M Tris buffer at pH 7.0 show a much slower exchange rate for mutant rHbs and Hb A. One of the mutants, rHb (beta131Gln --> Asn), shows the conformational exchange of its interface histidines, and exchange rate measurements have been attempted. We have also conducted studies on the reactivity of the SH group of beta93Cys (a residue located in the region of the alpha(1)beta(2)-subunit interface) toward p-mercuribenzoate, and our results show that low-oxygen-affinity rHbs have a more reactive beta93Cys than Hb A in the CO form. Our results indicate that there is communication between the alpha(1)beta(1)- and alpha(1)beta(2)-subunit interfaces, and a possible communication pathway for the cooperative oxygenation of Hb A that allows the alpha(1)beta(1)-subunit interface to modulate the functional properties in conjunction with the alpha(1)beta(2) interface is proposed.
[Mh] Termos MeSH primário: Substituição de Aminoácidos
Globinas/química
Hemoglobina A/química
[Mh] Termos MeSH secundário: Substituição de Aminoácidos/genética
Asparagina/genética
Sítios de Ligação/genética
Cisteína/química
Globinas/genética
Globinas/metabolismo
Glutamina/genética
Hemoglobina A/genética
Hemoglobina A/metabolismo
Histidina/química
Seres Humanos
Ligações de Hidrogênio
Mercurobenzoatos/química
Ressonância Magnética Nuclear Biomolecular/métodos
Oxigênio/metabolismo
Conformação Proteica
Prótons
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Relação Estrutura-Atividade
Reagentes de Sulfidrila/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (4-mercuribenzoate); 0 (Mercuribenzoates); 0 (Protons); 0 (Recombinant Proteins); 0 (Sulfhydryl Reagents); 0RH81L854J (Glutamine); 4QD397987E (Histidine); 7006-34-0 (Asparagine); 9004-22-2 (Globins); 9034-51-9 (Hemoglobin A); K848JZ4886 (Cysteine); S88TT14065 (Oxygen)
[Em] Mês de entrada:0205
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:020424
[St] Status:MEDLINE


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[PMID]:10708650
[Au] Autor:Mawjood AH; Miyazaki G; Kaneko R; Wada Y; Imai K
[Ad] Endereço:Department of Physiology and Biosignaling, Graduate School of Medicine, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
[Ti] Título:Site-directed mutagenesis in hemoglobin: test of functional homology of the F9 amino acid residues of hemoglobin alpha and beta chains.
[So] Source:Protein Eng;13(2):113-20, 2000 Feb.
[Is] ISSN:0269-2139
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The cysteine residue at F9(93) of the human hemoglobin (Hb A) beta chain, conserved in mammalian and avian hemoglobins, is located near the functionally important alpha1-beta2 interface and C-terminal region of the beta chain and is reactive to sulfhydryl reagents. The functional roles of this residue are still unclear, although regulation of local blood flow through allosteric S-nitrosylation of this residue is proposed. To clarify the role of this residue and its functional homology to F9(88) of the alpha chain, we measured oxygen equilibrium curves, UV-region derivative spectra, Soret-band absorption spectra, the number of titratable -SH groups with p-mercuribenzoate and the rate of reaction of these groups with 4, 4'-dipyridine disulfide for three recombinant mutant Hbs with single amino acid substitutions: Ala-->Cys at 88alpha (rHb A88alphaC), Cys-->Ala at 93beta (rHb C93betaA) and Cys-->Thr at 93beta (rHb C93betaT). These Hbs showed increased oxygen affinities and impaired allosteric effects. The spectral data indicated that the R to T transition upon deoxygenation was partially restricted in these Hbs. The number of titratable -SH groups of liganded form was 3.2-3.5 for rHb A88alphaC compared with 2.2 for Hb A, whereas those for rHb C93betaA and rHb C93betaT were negligibly small. The reduction of rate of reaction with 4,4'-dipyridine disulfide upon deoxygenation in rHb A88alphaC was smaller than that in Hb A. Our experimental data have shown that the residues at 88alpha and 93beta have definite roles but they have no functional homology. Structure-function relationships in our mutant Hbs are discussed.
[Mh] Termos MeSH primário: Hemoglobina A/química
Hemoglobina A/genética
Mutagênese Sítio-Dirigida
[Mh] Termos MeSH secundário: Regulação Alostérica
Substituição de Aminoácidos
Aminoácidos/química
Carboxihemoglobina/química
Cisteína/química
Seres Humanos
Concentração de Íons de Hidrogênio
Cinética
Espectrometria de Massas
Mercurobenzoatos/química
Mercurobenzoatos/metabolismo
Oxigênio/química
Oxigênio/metabolismo
Oxiemoglobinas/química
Oxiemoglobinas/genética
Proteínas Recombinantes
Espectrofotometria Ultravioleta
Relação Estrutura-Atividade
Compostos de Sulfidrila/química
Compostos de Sulfidrila/metabolismo
Reagentes de Sulfidrila/química
Reagentes de Sulfidrila/metabolismo
Titulometria
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Mercuribenzoates); 0 (Oxyhemoglobins); 0 (Recombinant Proteins); 0 (Sulfhydryl Compounds); 0 (Sulfhydryl Reagents); 9034-51-9 (Hemoglobin A); 9061-29-4 (Carboxyhemoglobin); K848JZ4886 (Cysteine); S88TT14065 (Oxygen)
[Em] Mês de entrada:0005
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:000310
[St] Status:MEDLINE


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[PMID]:9267326
[Au] Autor:Reddy PL; Bowie LJ; Callistein S
[Ad] Endereço:Clinical Laboratories, Evanston Hospital, IL 60201-1783, USA.
[Ti] Título:Binding of nitric oxide to thiols and hemes in hemoglobin H: implications for alpha-thalassemia and hypertension.
[So] Source:Clin Chem;43(8 Pt 1):1442-7, 1997 Aug.
[Is] ISSN:0009-9147
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Our earlier studies suggested an association between alpha-thalassemia and hypertension. We postulated that this association might involve trapping of the vasodilator nitric oxide (NO) by hemoglobin (Hb). Hb A has recently been shown to carry NO on its sulfhydryl groups in addition to its hemes. In this report we studied the interaction of purified Hb H as well as Hb A with NO. The number of reactive sulfhydryls were determined spectrophotometrically with bis-dithionitrobenzoate. Spectral studies and nitrosothiol measurements after treatment with NO or nitrosothiols indicated that all eight reactive sulfhydryls of Hb H were capable of binding NO. Hb A, however, was only able to bind and transfer two molecules of NO per tetramer. These findings support the biochemical basis for the association between alpha-thalassemia and hypertension.
[Mh] Termos MeSH primário: Hemoglobina H/metabolismo
Hipertensão/metabolismo
Óxido Nítrico/metabolismo
Talassemia alfa/metabolismo
[Mh] Termos MeSH secundário: Ácido Ditionitrobenzoico/metabolismo
Eletroforese em Gel de Ágar
Heme/metabolismo
Hemoglobina A/metabolismo
Hemoglobina H/química
Seres Humanos
Mercurobenzoatos/farmacologia
Compostos Nitrosos/análise
Oxigênio/metabolismo
Oxiemoglobinas/metabolismo
Nitrito de Sódio/metabolismo
Espectrofotometria
Compostos de Sulfidrila/análise
Compostos de Sulfidrila/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-mercuribenzoate); 0 (Mercuribenzoates); 0 (Nitroso Compounds); 0 (Oxyhemoglobins); 0 (Sulfhydryl Compounds); 31C4KY9ESH (Nitric Oxide); 42VZT0U6YR (Heme); 9034-51-9 (Hemoglobin A); 9034-79-1 (Hemoglobin H); 9BZQ3U62JX (Dithionitrobenzoic Acid); M0KG633D4F (Sodium Nitrite); S88TT14065 (Oxygen)
[Em] Mês de entrada:9709
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:970801
[St] Status:MEDLINE


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[PMID]:8885398
[Au] Autor:Venema K; Dost MH; Venema G; Kok J
[Ad] Endereço:Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Haren, The Netherlands.
[Ti] Título:Mutational analysis and chemical modification of Cys24 of lactococcin B, a bacteriocin produced by Lactococcus lactis.
[So] Source:Microbiology;142 ( Pt 10):2825-30, 1996 Oct.
[Is] ISSN:1350-0872
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Using site-directed mutagenesis the single cysteine residue at position 24 of lactococcin B was replaced by all other possible amino acids. Most of these mutant molecules retained bacteriocin activity, with the exception of those in which cysteine was replaced by a positively charged amino acid. This would seem to be in agreement with the authors' earlier observation that treatment of the wild-type molecule with HgCl2 resulted in its inactivation. The factor that causes inactivation of lactococcin B seems to be the introduction of a positive charge at position 24 by HgCl2 rather than oxidation of this residue, as treatment of the bacteriocin with other oxidative chemicals did not interfere with the ability of lactococcin B to dissipate the membrane potential of sensitive cells. Results are also reported which imply that inactive lactococcin B can still bind to its receptor. It can be replaced by an active bacteriocin molecule, resulting in dissipation of the membrane potential.
[Mh] Termos MeSH primário: Bacteriocinas/farmacologia
Cisteína/química
Lactococcus lactis/química
[Mh] Termos MeSH secundário: Bacteriocinas/química
Bacteriocinas/genética
Sulfato de Cobre/farmacologia
Cisteína/farmacologia
Cisteína/fisiologia
Ditiotreitol/farmacologia
Etilmaleimida/farmacologia
Formiatos/farmacologia
Lactococcus lactis/efeitos dos fármacos
Lactococcus lactis/genética
Lactococcus lactis/fisiologia
Potenciais da Membrana/efeitos dos fármacos
Mercurobenzoatos/farmacologia
Cloreto de Mercúrio/farmacologia
Mutagênese Sítio-Dirigida
Oxidantes/farmacologia
Oxirredução
Substâncias Redutoras/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (4-mercuribenzoate); 0 (Bacteriocins); 0 (Formates); 0 (Mercuribenzoates); 0 (Oxidants); 0 (Reducing Agents); 107-32-4 (peroxyformic acid); 145421-14-3 (lactococcin B); 53GH7MZT1R (Mercuric Chloride); K848JZ4886 (Cysteine); LRX7AJ16DT (Copper Sulfate); O3C74ACM9V (Ethylmaleimide); T8ID5YZU6Y (Dithiothreitol)
[Em] Mês de entrada:9701
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:961001
[St] Status:MEDLINE


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[PMID]:1612189
[Au] Autor:Parkhurst KM; Parkhurst LJ
[Ad] Endereço:Department of Chemistry, University of Nebraska, Lincoln 68588-0304.
[Ti] Título:Rapid preparation of native alpha and beta chains of human hemoglobin.
[So] Source:Int J Biochem;24(6):993-8, 1992 Jun.
[Is] ISSN:0020-711X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:1. Current procedures for the isolation of native chains of hemoglobin employ two ion exchange columns for each chain and result in readily autoxidizable chains with measurable contamination by Hb and Hg. 2. In the new procedure, altered buffer conditions on the first column reduce Hb contamination from 2 to 5% to less than 1%, the limit of detectability. 3. The second column and lengthy washes with beta mercaptoethanol are replaced by incubation with DTT for 1 min for alpha chains and, for beta chains, three incubations with DTT and separations by gel-filtration. The residual Hg is less than 0.1%. 4. Oxidations in the previous procedure resulted in low yields and unreliable spectroscopic assessments of bound Hg. The new procedure resulted in a simple UV assay for Hg-free chains. 5. Hemoglobin reconstituted from these oxy-chains was identical to native Hb in oxygen binding equilibria and in the kinetics of CO binding following laser photolysis.
[Mh] Termos MeSH primário: Hemoglobinas/isolamento & purificação
[Mh] Termos MeSH secundário: Cromatografia DEAE-Celulose
Cromatografia por Troca Iônica
Ditiotreitol
Hemoglobinas/química
Seres Humanos
Mercurobenzoatos/isolamento & purificação
Espectrofotometria Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Hemoglobins); 0 (Mercuribenzoates); T8ID5YZU6Y (Dithiothreitol)
[Em] Mês de entrada:9207
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:920601
[St] Status:MEDLINE


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[PMID]:2318835
[Au] Autor:Sivaram P; Deutscher MP
[Ad] Endereço:Department of Biochemistry, University of Connecticut Health Center, Farmington 06032.
[Ti] Título:Free fatty acids associated with the high molecular weight aminoacyl-tRNA synthetase complex influence its structure and function.
[So] Source:J Biol Chem;265(10):5774-9, 1990 Apr 05.
[Is] ISSN:0021-9258
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aminoacyl-tRNA synthetases from higher eukaryotes often are isolated as high molecular weight complexes associated with other components such as lipids. Since hydrophobic interactions are involved in the organization of the complex, it has been suggested that interaction of synthetases with these lipids might be important for their structure and function. Delipidation is known to affect certain properties of synthetases within the complex including sensitivity to detergents plus salts, temperature inactivation, hydrophobicity, sensitivity to proteases, and, as shown here, sensitivity to p-mercuribenzoate and sites of papain cleavage. Of the lipids known to co-purify with the complex, cholesterol esters, phospholipids and free fatty acids, we show that the particular lipids responsible for many of these changes are the free fatty acids. Specific removal of fatty acids results in a complex with properties similar to one totally delipidated by detergent treatment, and readdition of the fatty acid fraction reverses the effects. The fatty acid fraction contains both saturated and unsaturated fatty acids, but unsaturated fatty acids are much more effective in reversing the properties of the delipidated complex that are saturated fatty acids. These results indicate that the free fatty acids co-purifying with the synthetase complex bind to the synthetases and affect their structure and function.
[Mh] Termos MeSH primário: Aminoacil-tRNA Sintetases/metabolismo
Ácidos Graxos não Esterificados/metabolismo
[Mh] Termos MeSH secundário: Aminoacil-tRNA Sintetases/análise
Animais
Arginina-tRNA Ligase/metabolismo
Western Blotting
Fenômenos Químicos
Química Física
Cromatografia
Detergentes/farmacologia
Ácidos Graxos/farmacologia
Ácidos Graxos não Esterificados/análise
Ácidos Graxos não Esterificados/farmacologia
Feminino
Mercurobenzoatos/farmacologia
Peso Molecular
Papaína/metabolismo
Coelhos
Ratos
Ratos Endogâmicos
Relação Estrutura-Atividade
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (4-mercuribenzoate); 0 (Detergents); 0 (Fatty Acids); 0 (Fatty Acids, Nonesterified); 0 (Mercuribenzoates); EC 3.4.22.2 (Papain); EC 6.1.1.- (Amino Acyl-tRNA Synthetases); EC 6.1.1.19 (Arginine-tRNA Ligase)
[Em] Mês de entrada:9005
[Cu] Atualização por classe:161123
[Lr] Data última revisão:
161123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:900405
[St] Status:MEDLINE


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[PMID]:2302393
[Au] Autor:Clark SJ; Ralston GB
[Ad] Endereço:Department of Biochemistry, University of Sydney, Australia.
[Ti] Título:The dissociation of peripheral proteins from erythrocyte membranes brought about by p-mercuribenzenesulfonate.
[So] Source:Biochim Biophys Acta;1021(2):141-7, 1990 Jan 29.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The organic mercurial p-mercuribenzenesulfonate in 5 mM phosphate buffer (pH 8.0) solubilized ankyrin, bands 4.1 and 4.2, and glyceraldehyde-3-phosphate dehydrogenase from spectrin-depleted erythrocyte membranes. Glyceraldehyde-3-phosphate dehydrogenase was the protein most readily solubilized, being almost completely extracted by 0.5 mM reagent. The solubilization of ankyrin was similar to that of band 4.2, both showing maximal solubilization with 1.0 mM reagent. Band 4.1 was not appreciably solubilized below 2.5 mM p-mercuribenzenesulfonate. N-Ethylmaleimide did not itself solubilize proteins from ghosts or spectrin-depleted vesicles, and pretreatment at low temperature by 4 mM N-ethylmaleimide did not prevent subsequent solubilization by the mercurial. However, pretreatment at 37 degrees C with N-ethylmaleimide inhibited subsequent solubilization of ankyrin and band 4.2 by the mercurial and also resulted in the loss of binding of 1 mol mercurial per mol band 3. These data suggest that release of ankyrin and band 4.2 from the membrane by mercurial is linked to modification of band 3 by the reagent. After incubation of intact erythrocyte membranes with 0.1 M NaCl, treatment with p-mercuribenzenesulfonate selectively solubilized actin from the membranes. The resulting actin-depleted membranes did not vesiculate, but became spherical and lost their biconcave shape. Fragmentation was observed after subsequent removal of spectrin at low ionic strength.
[Mh] Termos MeSH primário: Proteínas do Citoesqueleto
Membrana Eritrocítica/análise
Proteínas de Membrana/sangue
Neuropeptídeos
[Mh] Termos MeSH secundário: Proteínas Sanguíneas/isolamento & purificação
Fracionamento Celular
Eletroforese em Gel de Poliacrilamida
Membrana Eritrocítica/enzimologia
Gliceraldeído-3-Fosfato Desidrogenases/sangue
Gliceraldeído-3-Fosfato Desidrogenases/isolamento & purificação
Seres Humanos
Proteínas de Membrana/isolamento & purificação
Mercurobenzoatos
Solubilidade
Espectrina/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (4-mercuribenzoate); 0 (Blood Proteins); 0 (Cytoskeletal Proteins); 0 (Membrane Proteins); 0 (Mercuribenzoates); 0 (Neuropeptides); 0 (erythrocyte membrane band 4.1 protein); 0 (erythrocyte membrane band 4.2 protein); 0 (erythrocyte membrane protein band 4.1-like 1); 12634-43-4 (Spectrin); EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases)
[Em] Mês de entrada:9003
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:900129
[St] Status:MEDLINE


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Fotocópia
[PMID]:2088881
[Au] Autor:Morgan DM
[Ad] Endereço:Section of Vascular Biology, M.R.C. Clinical Research Centre, Harrow, Middlesex, U.K.
[Ti] Título:Polyamine uptake by human vascular endothelial cells.
[So] Source:Biochem Soc Trans;18(6):1221-2, 1990 Dec.
[Is] ISSN:0300-5127
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Endotélio Vascular/metabolismo
Poliaminas/metabolismo
[Mh] Termos MeSH secundário: 2,4-Dinitrofenol
Transporte Biológico Ativo/efeitos dos fármacos
Células Cultivadas
Dinitrofenóis/farmacologia
Ditiotreitol/farmacologia
Endotélio Vascular/efeitos dos fármacos
Seres Humanos
Cinética
Mercurobenzoatos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-mercuribenzoate); 0 (Dinitrophenols); 0 (Mercuribenzoates); 0 (Polyamines); Q13SKS21MN (2,4-Dinitrophenol); T8ID5YZU6Y (Dithiothreitol)
[Em] Mês de entrada:9105
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:901201
[St] Status:MEDLINE



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