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1.
Proteins ; 92(7): 874-885, 2024 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-38477414

RESUMEN

Aquaporin (AQP) is a water channel protein from the family of transmembrane proteins which facilitates the movement of water across the cell membrane. It is ubiquitous in nature, however the understanding of the water transport mechanism, especially for AQPs in microbes adapted to low temperatures, remains limited. AQP also has been recognized for its ability to be used for water filtration, but knowledge of the biochemical features necessary for its potential applications in industrial processes has been lacking. Therefore, this research was conducted to express, extract, solubilize, purify, and study the functional adaptations of the aquaporin Z family from Pseudomonas sp. AMS3 via molecular approaches. In this study, AqpZ1 AMS3 was successfully subcloned and expressed in E. coli BL21 (DE3) as a recombinant protein. The AqpZ1 AMS3 gene was expressed under optimized conditions and the best optimized condition for the AQP was in 0.5 mM IPTG incubated at 25°C for 20 h induction time. A zwitterionic mild detergent [(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate was the suitable surfactant for the protein solubilization. The protein was then purified via affinity chromatography. Liposome and proteoliposome was reconstituted to determine the particle size using dynamic light scattering. This information obtained from this psychrophilic AQP identified provides new insights into the structural adaptation of this protein at low temperatures and could be useful for low temperature application and molecular engineering purposes in the future.


Asunto(s)
Acuaporinas , Proteínas Bacterianas , Clonación Molecular , Escherichia coli , Pseudomonas , Proteínas Recombinantes , Pseudomonas/metabolismo , Pseudomonas/genética , Pseudomonas/química , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismo , Proteínas Recombinantes/genética , Proteínas Recombinantes/aislamiento & purificación , Escherichia coli/genética , Escherichia coli/metabolismo , Acuaporinas/química , Acuaporinas/genética , Acuaporinas/metabolismo , Proteínas Bacterianas/química , Proteínas Bacterianas/genética , Proteínas Bacterianas/metabolismo , Expresión Génica , Proteolípidos/metabolismo , Proteolípidos/química , Regiones Antárticas , Liposomas/metabolismo , Liposomas/química , Agua/química , Agua/metabolismo , Solubilidad , Secuencia de Aminoácidos
2.
J Biomol Struct Dyn ; 41(21): 11498-11509, 2023.
Artículo en Inglés | MEDLINE | ID: mdl-36598349

RESUMEN

Aquaporin is a water channel protein that facilitates the movement of water across the cell membrane. Aquaporin from the Antarctic region has been noted for its psychrophilic properties and its ability to perform at a lower temperature but there remains limited understanding of the water mechanism of Antarctic Pseudomonas sp. strain AMS3 However, studies regarding aquaporin isolated from psychrophilic Pseudomonas sp. are still scattered. Recently, the genome sequence of an Antarctic Pseudomonas sp. strain AMS3 revealed a gene sequence encoding for a putative aquaporin designated as AqpZ1 AMS3. In this study, structure analysis and a molecular dynamics (MD) simulation of a predicted model of a fully hydrated aquaporin tetramer embedded in a lipid bilayer was performed at different temperatures for structural flexibility and stability analysis. The MD simulation results revealed that the structures were able to remain stable at low to medium temperatures. The protein was observed to have high flexibility in the loop region as compared to the helices region throughout the simulated temperatures. The selectivity filter and NPA motifs play a major role in solute selectivity and the pore radius of the protein. The structural and functional characterization of this psychrophilic aquaporin provides new insights for the future applications of this protein.Communicated by Ramaswamy H. Sarma.


Asunto(s)
Acuaporinas , Simulación de Dinámica Molecular , Regiones Antárticas , Pseudomonas/genética , Pseudomonas/metabolismo , Acuaporinas/química , Agua/química
3.
Int J Biol Macromol ; 180: 654-666, 2021 Jun 01.
Artículo en Inglés | MEDLINE | ID: mdl-33722623

RESUMEN

The present work developed porous carboxymethyl cellulose (CMC) carbon film from lignocellulosic based materials as supercapacitor electrode. Porous CMC carbon films of bamboo (B) and oil palm empty fruit bunch (O) were prepared through simple incipient wetness impregnation method followed by calcination process before incorporation with manganese oxide (Mn2O3). The carbonization produced porous CMC carbon whereby CMCB exhibited higher surface area than CMCO. After Mn2O3 incorporation, the crystallite size of CMCB and CMCO were calculated as 50.09 nm and 42.76 nm, respectively whereas Mn2O3/CMCB and Mn2O3/CMCO composite films were revealed to be 26.71 nm and 35.60 nm in size, respectively. Comparatively, the Mn2O3/CMCB composite film exhibited higher electrochemical performance which was 31.98 mF cm-2 as compared to 24.15 mF cm-2 by Mn2O3/CMCO composite film and both CMC carbon films with fairly stable cycling stability after 1000 charge-discharge cycles. Therefore, it can be highlighted that Mn2O3/CMC composite film as prepared from bamboo and oil palm fruit can potentially become the new electrode materials for supercapacitor application.


Asunto(s)
Carbono/química , Carboximetilcelulosa de Sodio/química , Celulosa/química , Lignina/química , Compuestos de Manganeso/química , Óxidos/química , Arecaceae/química , Celulosa/ultraestructura , Capacidad Eléctrica , Electrodos , Lignina/ultraestructura , Microscopía Electrónica de Rastreo/métodos , Microscopía Electrónica de Transmisión , Porosidad , Sasa/química
4.
East Mediterr Health J ; 15(5): 1098-104, 2009.
Artículo en Inglés | MEDLINE | ID: mdl-20214122

RESUMEN

Food-handlers (n = 1500) attending the public health laboratory in Khartoum, Sudan, for annual check-ups were screened for intestinal parasites by 3 different techniques (direct faecal examination, formol-ether concentration and floatation) to evaluate the adequacy of annual screening. Results showed that 29.4% of food-handlers were harbouring intestinal protozoa in stool samples: Entamoeba coli in 15.3%, Giardia lamblia in 9.7%, and Enta. histolytica in 4.3%. Moreover, 2.7% of food-handlers harboured intestinal helminths: Hymenolepis nana (1.6%), Schistosoma mansoni (0.7%), Taenia saginata (0.3%) and Strongyloides stercoralis (0.1%). We recommend more frequent screening of food-handlers and that the direct faecal smear technique is efficient for the detection of such parasites.


Asunto(s)
Heces/parasitología , Manipulación de Alimentos , Parasitosis Intestinales/diagnóstico , Parasitosis Intestinales/epidemiología , Tamizaje Masivo/métodos , Adulto , Distribución de Chi-Cuadrado , Colorantes , Éter , Femenino , Fijadores , Manipulación de Alimentos/estadística & datos numéricos , Formaldehído , Humanos , Parasitosis Intestinales/parasitología , Parasitosis Intestinales/transmisión , Yoduros , Masculino , Tamizaje Masivo/normas , Persona de Mediana Edad , Solventes , Sudán/epidemiología , Salud Urbana/estadística & datos numéricos , Sulfato de Zinc
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