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1.
Phlebology ; 26(7): 298-300, 2011 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-21576705

RESUMEN

AIM: The aim of this study was to investigate the effects of manual and mechanical lymph drainage on the bioelectrical composition of body tissues of patients with lymphoedema of the lower limbs. METHOD: Twenty-one patients with lymphoedema of one leg were evaluated using single frequency bioelectrical impedance with four electrodes (SF-BIA4) immediately before and after a combination of manual and mechanical lymph drainage. Statistical analysis used the two-tailed paired t-test with an alpha error of 5% being considered acceptable. RESULTS: On comparing the results before and after lymph drainage, statistically significant differences were identified for both lymphoedematous and apparently healthy legs, but there were no significant differences in the alterations caused by the treatment between the healthy and lymphoedematous limbs of the same patient. CONCLUSION: It was concluded that the association of manual and mechanical lymph drainage both modified the body composition as identified by bioelectrical impedance, and reduced the oedema.


Asunto(s)
Composición Corporal , Pierna/fisiopatología , Linfa , Linfedema/fisiopatología , Impedancia Eléctrica , Femenino , Humanos , Masculino
2.
Genet Mol Res ; 9(1): 360-4, 2010 Mar 02.
Artículo en Inglés | MEDLINE | ID: mdl-20309822

RESUMEN

The process of hemoglobin polymerization and the consequent sickling of red blood cells that occurs in patients with sickle cell disease shortens the half-life of red blood cells. It causes vaso-occlusive complications, as well as pain and pulmonary and cardiovascular dysfunction. We evaluated an aquatic rehabilitation program used for patients with sickle cell anemia and examined the possible benefits that exercise in warm water has for the circulatory system, for relieving pain, and for increasing lung capacity. The patient was a 32-year-old female. The parameters that we used in this study include respiratory muscle strength (which was calculated by measuring maximum inspiratory pressures and maximum expiratory pressures), the McGill and Wisconsin pain questionnaires (in order to evaluate the patients' characterizations and descriptions of their pain), and the SF-36 Health Survey. The treatment included warm water exercises, stretching, aerobic exercise, and relaxation, during two sessions of 45 min per week for 5 weeks. The patient experienced a significant decrease in pain, a significant increase in the strength of respiratory muscles, and improved quality of life. We conclude that aquatic rehabilitation can be used to improve the clinical condition of sickle cell anemia patients, and we encourage more research on this new treatment regime, in comparison with other types of therapies.


Asunto(s)
Anemia de Células Falciformes/fisiopatología , Anemia de Células Falciformes/rehabilitación , Hidroterapia , Cinestesia/fisiología , Adolescente , Adulto , Niño , Femenino , Humanos , Dimensión del Dolor , Encuestas y Cuestionarios
3.
Artículo en Inglés | MEDLINE | ID: mdl-16754983

RESUMEN

The cytochrome c nitrite reductase (cNiR) isolated from Desulfovibrio vulgaris Hildenborough is a membrane-bound complex formed of NrfA and NrfH subunits. The catalytic subunit NrfA is a soluble pentahaem cytochrome c that forms a physiological dimer of about 120 kDa. The electron-donor subunit NrfH is a membrane-anchored tetrahaem cytochrome c of about 18 kDa molecular weight and belongs to the NapC/NirT family of quinol dehydrogenases, for which no structures are known. Crystals of the native cNiR membrane complex, solubilized with dodecylmaltoside detergent (DDM), were obtained using PEG 4K as precipitant. Anomalous diffraction data were measured at the Swiss Light Source to 2.3 A resolution. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 79.5, b = 256.7, c = 578.2 A. Molecular-replacement and MAD methods were combined to solve the structure. The data presented reveal that D. vulgaris cNiR contains one NrfH subunit per NrfA dimer.


Asunto(s)
Citocromos a1/química , Citocromos c1/química , Desulfovibrio vulgaris/enzimología , Proteínas de la Membrana/química , Nitrato Reductasas/química , Membrana Celular/química , Cristalización/métodos , Subunidades de Proteína/química , Difracción de Rayos X
4.
Chembiochem ; 2(12): 895-905, 2001 Dec 03.
Artículo en Inglés | MEDLINE | ID: mdl-11948878

RESUMEN

A new tetraheme cytochrome c3 was isolated from the membranes of Desulfovibrio vulgaris Hildenborough (DvH). This cytochrome has a molecular mass of 13.4 kDa and a pI of 5.5 and contains four heme c groups with apparent reduction potentials of -170 mV, -235 mV, -260 mV and -325 mV at pH 7.6. The complete sequence of the new cytochrome, retrieved from the preliminary data of the DvH genome, shows that this cytochrome is homologous to the "acidic" cytochrome c3 from Desulfovibrio africanus (Da). A model for the structure of the DvH cytochrome was built based on the structure of the Da cytochrome. Both cytochromes share structural features that distinguish them from other cytochrome c3 proteins, such as a solvent-exposed heme 1 surrounded by an acidic surface area, and a heme 4 which lacks most of the surface lysine patch proposed to be the site of hydrogenase interaction in other cytochrome c3 proteins. Furthermore, in contrast to previously discovered cytochrome c3 proteins, the genes coding for these two cytochromes are adjacent to genes coding for two membrane-associated FeS proteins, which indicates that they may be part of membrane-bound oxidoreductase complexes. Altogether these observations suggest that the DvH and Da cytochromes are a new type of cytochrome c3 proteins (Type II: TpII-c3) with different redox partners and physiological function than the other cytochrome c3 proteins (Type I: TpI-c3). The DvH TpII-c3 is reduced at considerable rates by the two membrane-bound [NiFe] and [NiFeSe] hydrogenases, but catalytic amounts of TpI-c3 increase these rates two- and fourfold, respectively. With the periplasmic [Fe] hydrogenase TpII-c3 is reduced much slower than TpI-c3, and no catalytic effect of TpI-c3 is observed.


Asunto(s)
Grupo Citocromo c/química , Desulfovibrio vulgaris/química , Secuencia de Aminoácidos , Cromatografía en Agarosa , Cromatografía DEAE-Celulosa , Cromatografía Líquida de Alta Presión , Grupo Citocromo c/genética , Grupo Citocromo c/aislamiento & purificación , Desulfovibrio vulgaris/genética , Punto Isoeléctrico , Modelos Moleculares , Datos de Secuencia Molecular , Peso Molecular , Oxidación-Reducción , Conformación Proteica , Homología de Secuencia de Aminoácido , Espectrofotometría Ultravioleta
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