RESUMEN
BACKGROUND: Transfer of the flexor hallucis longus (FHL) tendon is a therapeutic option to replace a dysfunctional Achilles tendon in cases of rerupture with large defects, loss of the Achilles tendon after postoperative infection or severe tendinosis. MATERIALS AND METHODS: Between January 1994 and December 2005, 35 patients (5 female and 30 male, average age 47 years) were treated with 36 FHL transfers and 25 patients with 26 FHL transfers could be re-evaluated at a mean follow-up time of 79 months (range 20-133 months) after surgery. RESULTS: Of the 25 patients, 18 (72%) subjectively rated the result as excellent, 5 (20%) as good, and 1 patient (4%) each as fair and poor. According to the criteria of Trillat and Mournier-Kuhn, 18 patients (72%) were rated excellent, 4 (16%) good and 3 (12%) fair. The AOFAS ankle/hindfoot score at follow-up averaged 91 (range 13-100), the AOFAS forefoot score averaged 95 (range 24-100). CONCLUSIONS: FHL transfer to the Achilles tendon provides favorable results in cases of complicated cases with defects, infections or severe tendinosis after Achilles tendon rupture.
Asunto(s)
Tendón Calcáneo/lesiones , Tendón Calcáneo/cirugía , Traumatismos del Tobillo/cirugía , Transferencia Tendinosa/métodos , Traumatismos del Tobillo/diagnóstico , Femenino , Humanos , Masculino , Persona de Mediana Edad , Rotura/cirugía , Resultado del TratamientoRESUMEN
The effect of detergents and amphiphiles on protein solubility and their use in crystallization solutions was examined for an integral membrane protein, the light-harvesting I complex from Rhodospirillum centenum. Measurement by a centrifugation assay of the solubility of the protein in different detergents and amphiphiles showed high protein-solubility values when either octyl glucoside or lauryldimethylamine-N-oxide was present with heptanetriol or when deoxycholate was present with spermine. The detergent/amphiphile combinations that resulted in high protein solubility were shown to be successful for crystallization of the protein, suggesting that crystallization is favored for detergents and amphiphiles that optimize the solubility of integral membrane proteins. The amphiphiles effective for crystallization were found using laser mass spectrometry to displace the lauryldimethylamine-N-oxide bound to the protein. These results suggest that mass spectrometry can be used for screening of favorable crystallization conditions.
Asunto(s)
Detergentes/farmacología , Complejos de Proteína Captadores de Luz , Rhodospirillum centenum/química , Centrifugación , Cristalización , Ácido Desoxicólico/química , Dimetilaminas/química , Alcoholes Grasos/química , Glucósidos/química , Rayos Láser , Espectrometría de Masas , Proteínas/química , Espectrometría de Masa por Láser de Matriz Asistida de Ionización Desorción , Espermina/químicaRESUMEN
The relationship between the effect of detergents and amphiphiles on protein solubility and their use in crystallization solutions was examined for the reaction center from Rhodobacter sphaeroides. Measurement by a centrifugation assay of the solubility of the reaction center as a function of ionic strength revealed dramatic differences in the intrinsic solubility at zero ionic strength in the presence of various detergents and amphiphiles. High protein-solubility values were found for beta-octyl glucoside and for lauryldimethylamine-N-oxide with heptanetriol. The solubility differences are interpreted in terms of fundamental properties such as the polarity of the detergent molecules. Conditions that resulted in high protein solubility correspond to conditions that have been shown to be successful for crystallization of the reaction center. These results suggest that crystallization is favored for detergents and amphiphiles that optimize the solubility of integral membrane proteins.
Asunto(s)
Detergentes/química , Proteínas de la Membrana/química , Proteínas del Complejo del Centro de Reacción Fotosintética/química , Concentración Osmolar , Rhodobacter sphaeroides/química , SolubilidadRESUMEN
The effect of the amphiphile heptanetriol on the properties of solutions containing several detergents commonly used for crystallization of membrane proteins was characterized. The critical micelle concentration was found to be relatively unchanged by the presence of the amphiphile. In contrast, the addition of heptanetriol to solutions containing both detergent and polyethylene glycol exhibited significant shifts in the clouding behavior, with the largest shifts being for lauryl dimethylamine oxide. These results suggest that conditions favorable for crystallization of integral membrane proteins can be inferred from the properties of the detergents and amphiphiles.
Asunto(s)
Detergentes/química , Proteínas de la Membrana/química , Cristalización , Alcoholes Grasos/química , Micelas , Polietilenglicoles/química , TemperaturaRESUMEN
The reverse phase evaporation method was used to prepare lipid bilayer membrane vesicles containing 212Pb and other markers of high specific activity. Electron microscopy and microfiltration were used to measure the sizes of the liposomes. Isotopes were released from the liposomes during exposure to serum and this leakage was prevented by complexing of small molecules with proteins or by precipitating particulate complexes within the liposomes. The in vivo distribution of 212Pb liposomes differed from the distribution of free 212Pb in that the reticuloendothelial system cleared the liposomes. Liposomes with surface dinitrophenol hapten were highly immunogenic and the humoral response to dinitrophenol was nonspecifically suppressed by 212Pb liposomes.