Isolation and Characterization of a Lactose-Binding Lectin from Ocimum sanctum
نویسندگان
چکیده
منابع مشابه
Isolation, cloning and functional characterization of porcine mannose-binding lectin.
Binding of mannose-binding lectin (MBL), a C-type lectin, and its associated serine proteases, MASP-1 and MASP-2, to cell surface carbohydrates activates the lectin complement pathway. As MBL plays an important role in innate immunity, it has been cloned and characterized in several species. While the pig may be used as a source of organs/tissues for xenotransplantation, little is known about i...
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Andira anthelmia seeds, a species belonging to the Leguminosae family, Papilionoideae subfamily, Dalbergieae tribe, have a glucose/mannose specific lectin that agglutinates rabbit erythrocytes treated with trypsin. The Dalbergieae tribe has lectins which have specificity for different carbohydrates including mannose and also have several biological activities such as induction of rat paw edema,...
متن کاملOcimum sanctum - Tulsi PHARMACOLOGICAL ACTIONS AND USES
Ocimum sanctum is a widely branched, erect, stout and aromatic herb, about 75 cms high. This small herb is found throughout India and is cultivated near Hindu houses and temples. The leaves, seeds and root of this plant have been used in Ayurvedic medicine. The chemical composition of Tulsi is highly complex, containing many nutrients and other biological active compounds. Due to its inherent b...
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A lectin (BanLec-I) from banana (Musa paradisiac) with a binding specificity for oligomannosidic glycans of size classes higher than (Man)6GlcNAc was isolated and purified by affinity chromatography on a Sephadex G-75 column. It did not agglutinate untreated human or sheep erythrocytes, but it did agglutinate rabbit erythrocytes. BanLec-I stimulated T-cell proliferation. On size-exclusion chrom...
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Host cell invasion by Toxoplasma gondii is a multistep process with one of the first steps being the apical release of micronemal proteins that interact with host receptors. We demonstrate here that micronemal protein 1 (MIC1) is a lactose-binding lectin. MIC1 and MIC4 were recovered in the lactose-eluted (Lac(+)) fraction on affinity chromatography on immobilized lactose of the soluble antigen...
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ژورنال
عنوان ژورنال: Journal of Applied Pharmaceutical Science
سال: 2015
ISSN: 2231-3354
DOI: 10.7324/japs.2015.501019