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Bacteriophage-associated lyase activity against Klebsiella serotype K64 capsular polysaccharide

โœ Scribed by Neil Ravenscroft; Alistair M. Stephen; Edwin H. Merrifield


Book ID
102992380
Publisher
Elsevier Science
Year
1987
Tongue
English
Weight
689 KB
Volume
167
Category
Article
ISSN
0008-6215

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โœฆ Synopsis


Bacteriophage 464 possesses a lyase that depolymerises the capsular polysaccharide of Klebsiella K64 into a hexasaccharide having an unsaturated derivative of glucuronic acid at the non-reducing end (1). The unsaturated hex-4-enuronic acid residue generated was characterised spectroscopically (u.v. and n.m.r.) and by g.l.c.-m.s. after hydrogenation of the double bond. Partial hydrolysis, Smith degradation, methylation analysis, and n.m.r. spectroscopy have been used to establish the structures of oligosaccharides produced from the polysaccharide. Evidence from 'H-n.m.r. spectroscopy indicates that the D-Manp residue that undergoes fission is /3.


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