An investigation was made of the molecular weight of the Escherichia coil antigenic K5 polysaccharide. Two components with molecular weights of 16,000 and 1,500 were observed. The ratio of these two components depended on a lyase produced by the same E. coli. This lyase acts by a beta-elimination mechanism to depolymerize the K5. At the end of the fermentation the thermally treated (to inactivate the lyase) and untreated twenty-four-hour-old cultures each contained two K5 components of different M(w), in different ratios. The two components were monitored over a fermentation time-course. C-13-NMR spectrometry was employed to verify the lyase mechanism of action
The research presented in this thesis forms part of an on-going collaborative programme concerned wi...
of Escherichia coli by the K5-specific elimination) of the capsular K5 polysaccharide Analysis of th...
The Escherichia coli K4 bacterium (05:K4:H4) synthesizes a capsule polysaccharide with a carbohydrat...
ABSTRACT: The extracellular form of the K5 polysaccharide was produced, purified and characterized f...
The extracellular form of the K5 polysaccharide was produced, purified and characterized from a stra...
Escherichia coli K5 polysaccharide has structural analogies with N-acetylheparosan, a non-sulphated ...
Biosynthesis of the capsular K5 polysaccharide of Escherichia coli, which has the structure 4)-0GlcA...
I polisaccaridi capsulari di molti batteri gram negativi possono presentare attivita' antigene. L'an...
K5 lyase of coliphage K5A degrades the K5 polysaccharide of encapsulated E. coli strains expressing ...
The capsular polysaccharide of Escherichia coli K31 has been found by methylation analysis and n.m.r...
The production of the K4 polysaccharide was obtained for the first time extracellularly from a strai...
The structure of the capsular polysaccharide of Escherichia coli K5 is identical to that of N-acetyl...
Diseases caused by encapsulated bacteria such as E. coli are among the most prevalent in the world. ...
The capsular polysaccharide obtained from Escherichia coli K4 is a glycosaminoglycan-like molecule, ...
Group II K antigens such as the K5 are associated with Escherichia coli causing serious extraintesti...
The research presented in this thesis forms part of an on-going collaborative programme concerned wi...
of Escherichia coli by the K5-specific elimination) of the capsular K5 polysaccharide Analysis of th...
The Escherichia coli K4 bacterium (05:K4:H4) synthesizes a capsule polysaccharide with a carbohydrat...
ABSTRACT: The extracellular form of the K5 polysaccharide was produced, purified and characterized f...
The extracellular form of the K5 polysaccharide was produced, purified and characterized from a stra...
Escherichia coli K5 polysaccharide has structural analogies with N-acetylheparosan, a non-sulphated ...
Biosynthesis of the capsular K5 polysaccharide of Escherichia coli, which has the structure 4)-0GlcA...
I polisaccaridi capsulari di molti batteri gram negativi possono presentare attivita' antigene. L'an...
K5 lyase of coliphage K5A degrades the K5 polysaccharide of encapsulated E. coli strains expressing ...
The capsular polysaccharide of Escherichia coli K31 has been found by methylation analysis and n.m.r...
The production of the K4 polysaccharide was obtained for the first time extracellularly from a strai...
The structure of the capsular polysaccharide of Escherichia coli K5 is identical to that of N-acetyl...
Diseases caused by encapsulated bacteria such as E. coli are among the most prevalent in the world. ...
The capsular polysaccharide obtained from Escherichia coli K4 is a glycosaminoglycan-like molecule, ...
Group II K antigens such as the K5 are associated with Escherichia coli causing serious extraintesti...
The research presented in this thesis forms part of an on-going collaborative programme concerned wi...
of Escherichia coli by the K5-specific elimination) of the capsular K5 polysaccharide Analysis of th...
The Escherichia coli K4 bacterium (05:K4:H4) synthesizes a capsule polysaccharide with a carbohydrat...