Plant lectins are a heterogeneous group of proteins or glycoproteins that share in common their ability to recognize and bind specific sugar residues. At present hundreds of plant lectins have been isolated and characterized with respect to their molecular structures and carbohydrate-binding specificities. Since the unique biological properties of lectins can be exploited in the investigation of numerous biochemical and cellular phenomena, intense efforts are being made in many labs to isolate lectins with unique and unusual sugar-binding specificities. The study deals with the purification and partial characterization of a lectin from Crotalaria pallida belonging to Leguminoseae. Conformational changes and changes in biological properties by chemical modification of the lectin are also a part of the study. The lectin is a monomeric galactose and blood group A specific glycoprotein with about 4% carbohydrate and a molecular weight of 43 kDa. The activity yield of the lectin was about 4.6% with nearly three fold purification. Conformational changes were investigated by gel filtration, viscometery and UV absorption spectroscopy.
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La doctora Rabia Hamid, PhD en Bioquímica, es profesora asistente senior en el Departamento de Bioquímica de la Universidad de Cachemira. Actualmente su investigación se centra en las actividades antimicrobianas, antioxidantes y anticancerígenas de las lectinas vegetales y también de otros metabolitos secundarios de plantas medicinales de la región de Cachemira.
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Taschenbuch. Zustand: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Plant lectins are a heterogeneous group of proteins or glycoproteins that share in common their ability to recognize and bind specific sugar residues. At present hundreds of plant lectins have been isolated and characterized with respect to their molecular structures and carbohydrate-binding specificities. Since the unique biological properties of lectins can be exploited in the investigation of numerous biochemical and cellular phenomena, intense efforts are being made in many labs to isolate lectins with unique and unusual sugar-binding specificities. The study deals with the purification and partial characterization of a lectin from Crotalaria pallida belonging to Leguminoseae. Conformational changes and changes in biological properties by chemical modification of the lectin are also a part of the study. The lectin is a monomeric galactose and blood group A specific glycoprotein with about 4% carbohydrate and a molecular weight of 43 kDa. The activity yield of the lectin was about 4.6% with nearly three fold purification. Conformational changes were investigated by gel filtration, viscometery and UV absorption spectroscopy. 232 pp. Englisch. Bestandsnummer des Verkäufers 9783838371566
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Zustand: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: HAMID RABIADr.Rabia Hamid,Assistant Professor in the Department of Biochemistry, University of Kashmir, Srinagar has her area of research focussing on evaluation of medicinal properties of plant lectins. She has several research p. Bestandsnummer des Verkäufers 5417464
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Taschenbuch. Zustand: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Plant lectins are a heterogeneous group of proteins or glycoproteins that share in common their ability to recognize and bind specific sugar residues. At present hundreds of plant lectins have been isolated and characterized with respect to their molecular structures and carbohydrate-binding specificities. Since the unique biological properties of lectins can be exploited in the investigation of numerous biochemical and cellular phenomena, intense efforts are being made in many labs to isolate lectins with unique and unusual sugar-binding specificities. The study deals with the purification and partial characterization of a lectin from Crotalaria pallida belonging to Leguminoseae. Conformational changes and changes in biological properties by chemical modification of the lectin are also a part of the study. The lectin is a monomeric galactose and blood group A specific glycoprotein with about 4% carbohydrate and a molecular weight of 43 kDa. The activity yield of the lectin was about 4.6% with nearly three fold purification. Conformational changes were investigated by gel filtration, viscometery and UV absorption spectroscopy. Bestandsnummer des Verkäufers 9783838371566
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Taschenbuch. Zustand: Neu. Plant Lectins | A Biochemical study | Rabia Hamid (u. a.) | Taschenbuch | 232 S. | Englisch | 2010 | LAP LAMBERT Academic Publishing | EAN 9783838371566 | Verantwortliche Person für die EU: BoD - Books on Demand, In de Tarpen 42, 22848 Norderstedt, info[at]bod[dot]de | Anbieter: preigu. Bestandsnummer des Verkäufers 107491830
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Taschenbuch. Zustand: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Plant lectins are a heterogeneous group of proteins or glycoproteins that share in common their ability to recognize and bind specific sugar residues. At present hundreds of plant lectins have been isolated and characterized with respect to their molecular structures and carbohydrate-binding specificities. Since the unique biological properties of lectins can be exploited in the investigation of numerous biochemical and cellular phenomena, intense efforts are being made in many labs to isolate lectins with unique and unusual sugar-binding specificities. The study deals with the purification and partial characterization of a lectin from Crotalaria pallida belonging to Leguminoseae. Conformational changes and changes in biological properties by chemical modification of the lectin are also a part of the study. The lectin is a monomeric galactose and blood group A specific glycoprotein with about 4% carbohydrate and a molecular weight of 43 kDa. The activity yield of the lectin was about 4.6% with nearly three fold purification. Conformational changes were investigated by gel filtration, viscometery and UV absorption spectroscopy.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 232 pp. Englisch. Bestandsnummer des Verkäufers 9783838371566
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