Analysis of the lipopolysaccharide of Pseudomonas maltophilia 555

1987 ◽  
Vol 65 (11) ◽  
pp. 968-977 ◽  
Author(s):  
Jose L. Di Fabio ◽  
Malcolm B. Perry ◽  
David R. Bundle
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Brucella Species ◽  
Pseudomonas Maltophilia ◽  
Structure Formula ◽  
Derivatives Of ◽  
Acyl Derivatives

The phenol phase soluble lipopolysaccharide of Pseudomonas maltophilia strain 555, obtained from cells by the hot aqueous phenol method, was of the smooth type. Sodium dodecyl sulfate – polyacrylamide gel electrophoresis, hydrolysis, methylation, and 13C and 1H nuclear magnetic resonance analyses showed that this lipopolysaccharide has an O-chain polysaccharide composed of a repeating pentasaccharide unit, containing D-rhamnose (D-Rha, one part), 3-acetamido-3,6-dideoxy-D-galactose (D-Fuc3NAc, one part), and 4-acetamido-4,6-dideoxy-D-mannose (D-Rha4NAc, three parts) and having the structure[Formula: see text]The serological cross-reactions between P. maltophilia 555 and Brucella species can now be related to the occurrence of N-acyl derivatives of 4-amino-4,6-dideoxy-D-mannopyranosyl residues in the O-chains of their respective lipopolysaccharide components.

Structure of the antigenic O-polysaccharide of the lipopolysaccharide produced by Salmonella eimsbuttel

1988 ◽  
Vol 66 (2) ◽  
pp. 107-115 ◽  
Author(s):  
Jose L. Di Fabio ◽  
Malcolm B. Perry ◽  
Jean-Robert Brisson
Keyword(s):  
Molecular Weight ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Periodate Oxidation ◽  
Composition Analysis ◽  
Magnetic Resonance Studies ◽  
Structure Formula

The smooth lipopolysaccharide produced by Salmonella eimsbuttel, which had the O:6, O:7, and O:14 antigenic factors defined in the Kauffmann–White classification, was shown by sodium dodecyl sulfate – polyacrylamide gel electrophoresis analysis, composition analysis, methylation, periodate oxidation, deamination, and 1H and 13C nuclear magnetic resonance studies to contain a high molecular weight O-chain polysaccharide composed of D-mannose (four parts), D-glucose (one part), and 2-acetamido-2-deoxy-D-glucose (one part). It was a branched polymer of a repeating hexasaccharide unit having the structure[Formula: see text]

Catabolism of streptokinase and polyethylene glycol-streptokinase: evidence for transport of intact forms through the biliary system in the mouse

Blood ◽  
1990 ◽  
Vol 76 (1) ◽  
pp. 73-79 ◽  
Author(s):  
FH Brucato ◽  
SV Pizzo
Keyword(s):  
Molecular Weight ◽  
Polyethylene Glycol ◽  
Gel Electrophoresis ◽  
Proteinase Inhibitors ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gi Tract ◽  
Substantial Fraction ◽  
Sds Page ◽  
Derivatives Of

Abstract The catabolism of streptokinase (SK) and polyethylene glycol derivatives of SK (PEG-SK) were studied in mice. The clearance and catabolism of SK:plasmin (SK:Pm) and PEG-SK:Pm activator complexes were also investigated. Native 125I-SK cleared rapidly (t1/2 = 15 minutes) from the circulation, with the majority of the ligand accumulating in the liver and gastrointestinal (GI) tract and a substantial fraction also localizing in the kidneys. SK, which was removed from the plasma by the liver, was secreted into bile and then the GI tract. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that 125I-SK recovered from liver and bile was homogeneous and of the same molecular weight (mol wt approximately 50,200) as native SK. PEG-125I-SK cleared slowly (t1/2 greater than 200 minutes), with more than 80% of the preparation localizing in liver and GI tract. The PEG-125I-SK secreted into the bile was also intact. The bile containing 125I-SK was incubated with stoichiometric amounts of plasminogen and electrophoresed under nondenaturing conditions. This study demonstrated that the secreted SK was able to form SK:Pg complexes. SDS-PAGE also showed activation of 125I-Pg that was incubated with recovered bile containing the SK. 125I-SK:Pm catabolism was also studied. In these experiments, the mol wt approximately 42,000 fragment obtained when SK is cleaved by plasmin was found in the bile. This fragment of 125I-SK was not recovered as part of a complex with plasmin, consistent with our previous observations that catabolism of SK:Pm involves transfer of the plasmin to plasma proteinase inhibitors while SK is catabolized independently. By contrast, when PEG-125I-SK:Pm was injected into mice, only intact PEG-125I-SK was found in the bile, consistent with our previous observations that the PEG derivatization blocks its degradation by plasmin.

Structure of the O-chain of the lipopolysaccharide of Haemophilus pleuropneumoniae serotype 1

1986 ◽  
Vol 64 (12) ◽  
pp. 1317-1325 ◽  
Author(s):  
Eleonora Altman ◽  
Jean-Robert Brisson ◽  
Malcolm B. Perry
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Lipid A ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Two Dimensional ◽  
Magnetic Resonance Studies ◽  
Serotype 1 ◽  
Structure Formula ◽  
Phenol Water

By phenol-water extraction an aqueous-phase soluble cellular lipopolysaccharide was isolated from Haemophilus pleuropneumoniae serotype 1. It was shown by sodium dodecyl sulfate – polyacrylamide gel electrophoresis, hydrolysis, methylation, and both one- and two-dimensional 1H and 13C nuclear magnetic resonance studies to be an S-type lipopolysaccharide, which could be cleaved to yield a lipid A and an O-chain polysaccharide identified as a high molecular weight branched polymer of a tetrasaccharide repeating unit having the structure:[Formula: see text]

scholarly journals Catabolism of streptokinase and polyethylene glycol-streptokinase: evidence for transport of intact forms through the biliary system in the mouse

Blood ◽  
1990 ◽  
Vol 76 (1) ◽  
pp. 73-79
Author(s):  
FH Brucato ◽  
SV Pizzo
Keyword(s):  
Molecular Weight ◽  
Polyethylene Glycol ◽  
Gel Electrophoresis ◽  
Proteinase Inhibitors ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gi Tract ◽  
Substantial Fraction ◽  
Sds Page ◽  
Derivatives Of

The catabolism of streptokinase (SK) and polyethylene glycol derivatives of SK (PEG-SK) were studied in mice. The clearance and catabolism of SK:plasmin (SK:Pm) and PEG-SK:Pm activator complexes were also investigated. Native 125I-SK cleared rapidly (t1/2 = 15 minutes) from the circulation, with the majority of the ligand accumulating in the liver and gastrointestinal (GI) tract and a substantial fraction also localizing in the kidneys. SK, which was removed from the plasma by the liver, was secreted into bile and then the GI tract. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that 125I-SK recovered from liver and bile was homogeneous and of the same molecular weight (mol wt approximately 50,200) as native SK. PEG-125I-SK cleared slowly (t1/2 greater than 200 minutes), with more than 80% of the preparation localizing in liver and GI tract. The PEG-125I-SK secreted into the bile was also intact. The bile containing 125I-SK was incubated with stoichiometric amounts of plasminogen and electrophoresed under nondenaturing conditions. This study demonstrated that the secreted SK was able to form SK:Pg complexes. SDS-PAGE also showed activation of 125I-Pg that was incubated with recovered bile containing the SK. 125I-SK:Pm catabolism was also studied. In these experiments, the mol wt approximately 42,000 fragment obtained when SK is cleaved by plasmin was found in the bile. This fragment of 125I-SK was not recovered as part of a complex with plasmin, consistent with our previous observations that catabolism of SK:Pm involves transfer of the plasmin to plasma proteinase inhibitors while SK is catabolized independently. By contrast, when PEG-125I-SK:Pm was injected into mice, only intact PEG-125I-SK was found in the bile, consistent with our previous observations that the PEG derivatization blocks its degradation by plasmin.

Structural studies of the O-chain of the phenol-phase soluble lipopolysaccharide from Haemophilus pleuropneumoniae serotype 2

1987 ◽  
Vol 65 (10) ◽  
pp. 876-889 ◽  
Author(s):  
Eleonora Altman ◽  
Jean-Robert Brisson ◽  
David R. Bundle ◽  
Malcolm B. Perry
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Lipid A ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Two Dimensional ◽  
Structural Studies ◽  
Magnetic Resonance Studies ◽  
Structure Formula ◽  
Phenol Water

The phenol-phase soluble cellular lipopolysaccharide that was isolated by the phenol–water extraction from Haemophilus pleuropneumoniae serotype 2 was shown to be of the S type by sodium dodecyl sulfate – polyacrylamide gel electrophoresis, hydrolysis, methylation, specific degradations, and both one- and two-dimensional 1H and 13C nuclear magnetic resonance studies. It could be cleaved to yield a lipid A and an O-chain polysaccharide. This O-polysaccharide was identified as a high molecular weight unbranched linear polymer of a pentasaccharide repeating unit having the structure:[Formula: see text]

Administration of a creatine analogue induces isomyosin transitions in muscle

1989 ◽  
Vol 257 (4) ◽  
pp. C810-C816 ◽  
Author(s):  
T. S. Moerland ◽  
N. G. Wolf ◽  
M. J. Kushmerick
Keyword(s):  
Physical Activity ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Gel Electrophoresis ◽  
Extensor Digitorum Longus ◽  
Sodium Dodecyl ◽  
Serum Glucose ◽  
Relative Content ◽  
Heart Ventricle ◽  
Hindlimb Muscle

A creatine analogue, beta-guanidinopropionic acid (beta-GPA), was administered in the food (2% wt/wt) and the water (0.5% wt/vol) of male CD-1 mice. Uptake of the phosphorylated analogue and depletion of phosphocreatine in hindlimb muscle was monitored by 31P nuclear magnetic resonance and was found to be complete within 7 wk. After this time, the isomyosin composition of soleus, extensor digitorum longus (EDL), and ventricle was analyzed by pyrophosphate gel electrophoresis. The analogue was found to induce significant alterations in the type of myosin expressed in soleus and EDL. Normal soleus contains both intermediate (IM) and slow (SM) myosins, and treatment reduced the relative content of IM by approximately 50%. In EDL, treatment decreased fast isomyosin FM3 by 60% compared with controls. Sodium dodecyl sulfate-gel electrophoresis also showed a decrease of parvalbumin in EDL by approximately 50%. Treatment had no significant effect on the isomyosin composition of heart ventricle. Levels of physical activity and concentrations of serum glucose and thyroxine of treated mice were not significantly different from controls. These results indicate a role for intracellular energetics in mediating adaptive changes in the phenotype of muscle in mature animals.

Structure of the glycan chain from the surface layer glycoprotein of Bacillus alvei CCM 2051

1991 ◽  
Vol 69 (1) ◽  
pp. 72-78 ◽  
Author(s):  
Eleonora Altman ◽  
Jean-Robert Brisson ◽  
Paul Messner ◽  
Uwe B. Sleytr
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Surface Layer ◽  
Magnetic Resonance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Glycan Chain ◽  
Molecular Masses ◽  
Nuclear Magnetic

The cell surface of the mesophilic eubacterium Bacillus alvei CCM 2051 is covered by an oblique arranged surface layer glycoprotein. The subunits revealed by sodium dodecyl sulfate – polyacrylamide gel electrophoresis were distinct bands of molecular masses 140 000, 128 000, and 127 000. Proteolytic degradation of the purified S-layer glycoprotein yielded a single glycopeptide fraction with an apparent molecular mass of ca. 25 000. Methylation analysis in conjunction with two-dimensional nuclear magnetic resonance experiments at 500 MHz established the branched trisaccharide[Formula: see text]as the repeating unit for this glycan chain.Key words: surface layer, eubacteria, glycoprotein, nuclear magnetic resonance, structure.

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