Bacteriophage-borne enzymes in carbohydrate chemistry. Part I. On the glycanase activity associated with particles of Klebsiella bacteriophage No. 11.
Carbohydr Res, 1975/5;41:257-71.
PMID: 236830
Impact factor: 2.975
Abstract
The preparation and use of particles of Klebsiella bacteriophage No. 11 are described. A glycanase activity associated with the viruses catalyses the depolymerization of (alkali-treated) Klebsiella serotype 11 capsular polysaccharide, ultimately to a mixture of oligosaccharides consisting of one or two repeating units. Mainly glucosidic bonds are hydrolysed. The substrate specificity of the viral enzyme has been characterized by using derivatives of serotype-11 polysaccharide, as well as 81 heterologous, bacterial, capsular glycans. It is concluded that the glycanase will (at least) also depolymerize all polysaccharides containing the unsubstituted chain-trisaccharide repeating-unit of its natural substrate.
MeSH terms
Aluminum; Antigens; Bacteriophages; Blood Group Antigens; Chromatography, Ion Exchange; Drug Stability; Glycoside Hydrolases; Hydrogen-Ion Concentration; Kinetics; Klebsiella; Lithium; Oligosaccharides; Polysaccharides, Bacterial; Species Specificity; Temperature; Viral Plaque Assay
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