Results 131 to 140 of about 77,033 (163)
Comparative genomics of aflatoxigenic A. flavus reveals mycotoxin diversity and postharvest adaptation in cashew nuts from coastal Kenya. [PDF]
Katua K +8 more
europepmc +1 more source
Comparative genomics reveals the molecular basis for divergent algicidal strategies in two <i>Alteromonas macleodii</i> strains. [PDF]
Lai Y, Liu X, Chen Z, Li Y, Shi X.
europepmc +1 more source
Action pattern of polysaccharide lyases on glycosaminoglycans
The action pattern of polysaccharide lyases on glycosaminoglycan substrates was examined using viscosimetric measurements and gradient polyacrylamide gel electrophoresis (PAGE). Heparin lyase I (heparinase, EC 4.2.2.7) and heparin lyase II (no EC number) both acted on heparin in a random endolytic fashion.
Robert Linhardt
exaly +4 more sources
Analysis of Glycosaminoglycans with Polysaccharide Lyases
Polysaccharide lyases are a class of enzymes useful for analysis of glycosaminoglycans (GAGs) and the glycosaminoglycan component of proteoglycans (PGs). These enzymes cleave specific glycosidic linkages present in acidic polysaccharides and result in depolymerization.
Robert J. Linhardt, Linhardt, Robert J.
exaly +4 more sources
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Applied Biochemistry and Biotechnology, 1987
Polysaccharide lyases (or eliminases) are a class of enzymes (EC 4.2.2.-) that act to cleave certain activated glycosidic linkages present in acidic polysaccharides. These enzymes act through an eliminase mechanism, rather than through hydrolysis, resulting in unsaturated oligosaccharide products.
Robert Linhardt, Charles L Cooney
exaly +3 more sources
Polysaccharide lyases (or eliminases) are a class of enzymes (EC 4.2.2.-) that act to cleave certain activated glycosidic linkages present in acidic polysaccharides. These enzymes act through an eliminase mechanism, rather than through hydrolysis, resulting in unsaturated oligosaccharide products.
Robert Linhardt, Charles L Cooney
exaly +3 more sources
Polysaccharide Lyases: Recent Developments as Biotechnological Tools
Critical Reviews in Biotechnology, 2003Polysaccharide lyases, which are polysaccharide cleavage enzymes, act mainly on anionic polysaccharides. Produced by prokaryote and eukaryote organisms, these enzymes degrade (1,4) glycosidic bond by a beta elimination mechanism and have unsaturated oligosaccharides as major products.
Philippe Michaud, J Courtois
exaly +3 more sources
Carbohydrate Research, 2004
A thio-linked disaccharide based on the structure of the glycosaminoglycan chondroitin was synthesized as a potential inhibitor of chondroitin AC lyase from Flavobacterium heparinum for structural analysis of the active site. Instead it was found to be a slow substrate, thereby demonstrating that lyases, in contrast to glycosidases, can cleave ...
Stephen Withers
exaly +3 more sources
A thio-linked disaccharide based on the structure of the glycosaminoglycan chondroitin was synthesized as a potential inhibitor of chondroitin AC lyase from Flavobacterium heparinum for structural analysis of the active site. Instead it was found to be a slow substrate, thereby demonstrating that lyases, in contrast to glycosidases, can cleave ...
Stephen Withers
exaly +3 more sources
Carbohydrate-active enzymes (CAZymes) are an important characteristic of bacteria in marine systems. We herein describe the CAZymes of Paenibacillus algicola HB172198(T), a novel type species isolated from brown algae in Qishui Bay, Hainan, China.
Zixu Wang, Huiqin Huang, Yonghua Hu
exaly +2 more sources

