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1.
AORN J ; 53(6): 1480-96, 1991 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-1863065

RESUMO

As techniques become more advanced, perioperative nurses in all surgical specialties must increase their knowledge to provide safe patient care. Cardiopulmonary bypass for cardiac surgery demands special knowledge and skills. Knowledge of the principles of CPB allows the nurse to give excellent nursing care and to function as an effective member of the health care team.


Assuntos
Ponte Cardiopulmonar/enfermagem , Enfermagem de Centro Cirúrgico/métodos , Soluções Cardioplégicas/química , Ponte Cardiopulmonar/instrumentação , Ponte Cardiopulmonar/métodos , Educação Continuada em Enfermagem , Humanos , Cuidados Intraoperatórios/métodos , Cuidados Pós-Operatórios/métodos , Cuidados Pré-Operatórios/métodos
2.
J Bacteriol ; 172(7): 3826-9, 1990 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-2193917

RESUMO

Energy-coupled reactions of the Escherichia coli outer membrane transport proteins BtuB and Cir require the tonB product. Some point mutations in a region of btuB and cir that is highly conserved in TonB-dependent transport proteins led to loss of TonB-coupled uptake of vitamin B12 and colicin Ia, whereas binding was unaffected. Most other point mutations in this region had no detectable effect on transport activity. Mutations in tonB that suppressed the transport defect phenotype of these btuB mutations were isolated. All carried changes of glutamine 165 to leucine, lysine, or proline. The various tonB mutations differed markedly in their suppression activities on different btuB or cir mutations. This allele specificity of suppression indicates that TonB interacts directly with the outer membrane transport proteins in a manner that recognizes the local conformation but not specific side chains within this conserved region. An effect of the context of the remainder of the protein was seen, since the same substitution (valine 10----glycine) in btuB and cir responded differently to the suppressors. This finding supports the proposal that TonB interacts with more of the transport proteins than the first conserved domain alone.


Assuntos
Proteínas da Membrana Bacteriana Externa/genética , Proteínas de Bactérias/genética , Proteínas de Escherichia coli , Escherichia coli/genética , Proteínas de Membrana/genética , Supressão Genética , Alelos , Proteínas da Membrana Bacteriana Externa/metabolismo , Proteínas de Bactérias/metabolismo , Sequência de Bases , Transporte Biológico , Escherichia coli/metabolismo , Genes Bacterianos , Proteínas de Membrana/metabolismo , Dados de Sequência Molecular , Mutação , Sondas de Oligonucleotídeos
3.
J Bacteriol ; 171(12): 6526-33, 1989 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-2687240

RESUMO

Uptake of cobalamins and iron chelates in Escherichia coli K-12 is dependent on specific outer membrane transport proteins and the energy-coupling function provided by the TonB protein. The btuB product is the outer membrane receptor for cobalamins, bacteriophage BF23, and the E colicins. A short sequence near the amino terminus of mature BtuB, previously called the TonB box, is conserved in all tonB-dependent receptors and colicins and is the site of the btuB451 mutation (Leu-8----Pro), which prevents energy-coupled cobalamin uptake. This phenotype is partially suppressed by certain mutations in tonB. To examine the role of individual amino acids in the TonB box of BtuB, more than 30 amino acid substitutions in residues 6 to 13 were generated by doped oligonucleotide-directed mutagenesis. Many of the mutations affecting each amino acid did not impair transport activity, although some substitutions reduced cobalamin uptake and the Leu-8----Pro and Val-10----Gly alleles were completely inactive. To test whether the btuB451 mutation affects only cobalamin transport, a hybrid gene was constructed which encodes the signal sequence and first 39 residues of BtuB fused to the bulk of the ferrienterobactin receptor FepA (residues 26 to 723). This hybrid protein conferred all FepA functions but no BtuB functions. The presence of the btuB451 mutation in this fusion gene eliminated all of its tonB-coupled reactions, showing that the TonB box of FepA could be replaced by that from BtuB. These results suggest that the TonB-box region of BtuB is involved in active transport in a manner dependent not on the identity of specific side chains but on the local secondary structure.


Assuntos
Proteínas da Membrana Bacteriana Externa/genética , Escherichia coli/genética , Mutação , Vitamina B 12/metabolismo , Sequência de Aminoácidos , Proteínas da Membrana Bacteriana Externa/metabolismo , Sequência de Bases , Transporte Biológico , Quimera , Códon/genética , Escherichia coli/metabolismo , Genótipo , Cinética , Dados de Sequência Molecular , Sondas de Oligonucleotídeos , Plasmídeos
4.
Kidney Int ; 34(5): 683-90, 1988 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-2974094

RESUMO

Autosomal dominant polycystic kidney disease (ADPKD) has been shown to be associated with a greater than 50 percent incidence of hypertension prior to deterioration in renal function as assessed by glomerular filtration rate. The present study provides evidence for increased cardiac pre-load, as assessed by plasma atrial natriuretic factor (ANF) and cardiac index, in hypertensive as compared to normotensive ADPKD. The hypertensive ADPKD patients exhibited an increased renal vascular resistance as compared to the normotensive patients in spite of comparable glomerular filtration rates. It is hypothesized that the renal involvement of hypertensive ADPKD patients causes an impaired renal response to the observed increase in cardiac index, and also may release a venoconstrictor (such as angiotensin) which contributes to the enhanced cardiac pre-load and thus the hypertension.


Assuntos
Genes Dominantes , Hipertensão Renal/etiologia , Doenças Renais Policísticas/genética , Sistema Renina-Angiotensina , Adulto , Fator Natriurético Atrial/sangue , Débito Cardíaco , Feminino , Humanos , Hipertensão Renal/fisiopatologia , Masculino , Pessoa de Meia-Idade , Natriurese , Volume Plasmático , Doenças Renais Policísticas/complicações , Sódio na Dieta/administração & dosagem
5.
Appl Environ Microbiol ; 53(11): 2610-6, 1987 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-16347480

RESUMO

Several anaerobic bacteria isolated from the sediments of Contrary Creek, an iron-rich environment, produced magnetite when cultured in combinations but not when cultured alone in synthetic iron oxyhydroxide medium. When glucose was added as a carbon source, the pH of the medium decreased (to 5.5) and no magnetite was formed. When the same growth medium without glucose was used, the pH increased (to 8.5) and magnetite was formed. In both cases, Fe was released into the growth medium. Geochemical equilibrium equations with E(h) and pH as master variables were solved for the concentrations of iron and inorganic carbon that were observed in the system. Magnetite was predicted to be the dominant iron oxide formed at high pHs, while free Fe or siderite were the dominant forms of iron expected at low pHs. Thus, magnetite formation occurs because of microbial alteration of the local E(h) and pH conditions, along with concurrent reduction of ferric iron (direct biological reduction or abiological oxidation-reduction reactions).

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