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Article Dans Anglais | IMSEAR | ID: sea-162005

Résumé

Aegle marmelos (Rutaceae) is being used in traditional medicine treatments, such as for intermittent fever, intestinal ailments, fertility control etc. It has been proved to be effective against several major diseases including cancer, diabetis and cardiovascular diseases. Although the plant is a well known male antifertility plant, till today only the crude extracts of the plant were screened for antifertility activity in male rats. The plant is rich in alkaloid content and Aegelenine, Marmeline and Skimmianine, are some of the alkaloids isolated so far, showed variety of pharmacological activities. In view of these facts, in the present study, total alkaloids have been isolated from leaves of A. marmelos and their effect on fertility of adult male albino rats (Rattus norvegicus) was investigated. Three different doses 20, 40, 80 mg/kg body weight of total alkaloids were orally administered to mature male albino rats (Wistar strain) of proven fertility (235-2450gr) for 60 days. On day 61, all the animals were sacrificed and the fertility and safety parameters were studied. Weights of all the major reproductive organs, accessory glands and sperm counts were significantly decreased in dose dependent manner suggesting the antifertility activity and serological parameters showed no significant changes in treated animals at the tested dose levels indicating the safety of long-term use of total alkaloidal fraction of A. marmelos.

2.
Article Dans Anglais | IMSEAR | ID: sea-161288

Résumé

Riboflavin binding protein (RfBP) was isolated, purified and characterized from Hen (Gallus gallus) egg white and yolk using Sepharose column chromatography. The Rfbp was purified using DEAE-Sepharose ion exchange chromatography followed by gel filtration on Sephadex G-100. The protein content was estimated with Lowry method. The purity of the proteins was judged by SDS-PAGE technique. The protein migrated as a single band on SDS gel with a molecular weight of 29 kilodaltons. This is the first report on purification of this protein using DEAE-Sepharose column chromatography.

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