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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Dr.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 papers and review articles to her credit in reputed journals and is on the Board of Reviewers of some international journals.
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Seller: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Germany
Taschenbuch. Condition: 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. Seller Inventory # 9783838371566
Seller: moluna, Greven, Germany
Condition: 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. Seller Inventory # 5417464
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Seller: AHA-BUCH GmbH, Einbeck, Germany
Taschenbuch. Condition: 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. Seller Inventory # 9783838371566
Seller: preigu, Osnabrück, Germany
Taschenbuch. Condition: 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. Seller Inventory # 107491830
Seller: buchversandmimpf2000, Emtmannsberg, BAYE, Germany
Taschenbuch. Condition: 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. Seller Inventory # 9783838371566