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1.
Proteins ; 56(4): 821-7, 2004 Sep 01.
Artículo en Inglés | MEDLINE | ID: mdl-15281133

RESUMEN

The three-dimensional structure of the recombinant form of Erythrina corallodendron lectin, complexed with lactose, has been elucidated by X-ray crystallography at 2.55 A resolution. Comparison of this non-glycosylated structure with that of the native glycosylated lectin reveals that the tertiary and quaternary structures are identical in the two forms, with local changes observed at one of the glycosylation sites (Asn17). These changes take place in such a way that hydrogen bonds with the neighboring protein molecules in rECorL compensate those made by the glycan with the protein in ECorL. Contrary to an earlier report, this study demonstrates that the glycan attached to the lectin does not influence the oligomeric state of the lectin. Identical interactions between the lectin and the non-covalently bound lactose in the two forms indicate, in line with earlier reports, that glycosylation does not affect the carbohydrate specificity of the lectin. The present study, the first of its kind involving a glycosylated protein with a well-defined glycan and the corresponding deglycosylated form, provides insights into the structural aspects of protein glycosylation.


Asunto(s)
Lectinas de Plantas/química , Lectinas de Plantas/metabolismo , Sitios de Unión , Metabolismo de los Hidratos de Carbono , Cristalografía por Rayos X , Glicosilación , Lactosa/química , Lactosa/metabolismo , Lectinas/química , Lectinas/metabolismo , Estructura Cuaternaria de Proteína , Estructura Terciaria de Proteína , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismo
2.
Placenta ; 21(2-3): 234-40, 2000.
Artículo en Inglés | MEDLINE | ID: mdl-10736247

RESUMEN

The oxidation of eugenol by purified human term placental peroxidase (HTPP) was examined. Spectral analyses indicated that, similar to horseradish peroxidase, HTPP is capable of catalyzing the oxidation of eugenol. The accumulated stable product in the reaction medium due to eugenol oxidation by HTPP was tentatively identified as quinone methide of eugenol (EQM). The EQM formation exhibited a pH optimum of 8.0 and was dependent on incubation time, amount of HTPP and the concentration of both eugenol and hydrogen peroxide. The specific activity of approx 2.8 micromoles of EQM/min/mg protein was observed with different preparations of HTPP. The EQM formation was significantly suppressed by glutathione and ascorbic acid. The classical peroxidase inhibitors viz. potassium cyanide and sodium azide blocked the reaction in a concentration manner. Collectively, the results suggest that eugenol may undergo peroxidative metabolism in human placenta.


Asunto(s)
Eugenol/metabolismo , Peroxidasas/metabolismo , Placenta/enzimología , Eugenol/química , Femenino , Peroxidasa de Rábano Silvestre/metabolismo , Humanos , Técnicas In Vitro , Oxidación-Reducción , Peroxidasas/aislamiento & purificación , Embarazo , Espectrofotometría , Espectrofotometría Ultravioleta
3.
Int J Vitam Nutr Res ; 47(4): 389-93, 1977.
Artículo en Inglés | MEDLINE | ID: mdl-591211

RESUMEN

Hematological studies were carried out in 110 children with varying levels of plasma retinol to investigate the relationship between vitamin A deficiency and anemia. In children with plasma retinol levels below 20 microgram/100 ml, the mean levels of hemoglobin and hematocrit were lower than those in children who had retinol levels above 20 microgram/100 ml. Following supplementation of vitamin A, there was a significant increase in the levels of hemoglobin, hematocrit and plasma iron. These findings suggest that apart from deficiency of iron, vitamin A deficiency may also have a contributory role in the development of anemia in children.


Asunto(s)
Eritrocitos , Hemoglobinas , Hierro/sangre , Deficiencia de Vitamina A/sangre , Niño , Hematócrito , Hemoglobinas/análisis , Humanos , Fenómenos Fisiológicos de la Nutrición , Vitamina A/sangre , Vitamina A/uso terapéutico , Deficiencia de Vitamina A/tratamiento farmacológico
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