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salmonella infections/albumina

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Immunization of rabbits with the synthetic disaccharide-protein conjugate, tyvelose 1 leads to alpha 3 mannose 1 leads to bovine serum albumin (TM-BSA) in Freund's complete adjuvant, gave rise to antibodies directed against both the disaccharide hapten and the carrier protein. The hapten antibodies
The octasaccharide Galp (Formula: see text) Rhap, the synthesized disaccharides methyl 3-O-a-tyvelopyranosyl-a-D-mannopyranoside, methyl 3-O-a-tyvelopyranosyl-beta-D-mannopyranoside and methyl alpha-tyveloside, in order of decreasing effectiveness, inhibited the precipitation of S. typhi T2
Lipopolysaccahrides (LPSs) from Salmonella enteritidis, S. gallinarum, and S. enterica Typhimurium showed an identical electrophoretic banding pattern and serological cross-reactions among each other. LPSs from wild-type Salmonella enteritidis and rough mutant S. gallinarum 9R were detoxified by
The O-antigenic polysaccharide of phenol-water extracted Salmonella typhimurium (O antigens 4, 12) lipopolysaccharide was enzymatically cleaved by phage P22 endorhamnosidase. An octasaccharide with the (formula: see text) structure Gal-Man-Rha-Gal-Man-Rha was isolated and shown to retain the
Antiserum specific for Salmonella O3 antigen was raised by immunization of rabbits with an artificial glycoconjugate consisting of the synthetic trisaccharide beta-D- Manp (1----4)-alpha-L- Rhap (1----3)-alpha-D-Galp covalently linked to bovine serum albumin (beta- MRG -BSA). Enzyme immunoassays
The binding specificities of antibodies directed against the Salmonella sero-group A-specific O-antigen 2 determinant were characterized by precipitation-inhibition and enzyme-linked immunosorbent assay inhibition tests. Two different antigen O-2-specific antisera were investigated: one conventional
Secretion rates of immunoglobulins and other proteins were assessed by luminal perfusion of jejunum and distal ileum, and the jejunal histology was evaluated in eight Danish chronic Salmonella typhi and paratyphi carriers compared to nine healthy controls who previously had suffered from typhoid or

Agglutinating antiserum for the isolation of Salmonella with special reference to isolation from egg albumin.

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Protection against mouse typhoid by artificial Salmonella vaccines.

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Salmonella serogroup BO antigen specific octasaccharides were isolated from phage P22 endo-rhamnosidase cleaved S. typhimurium O-polysaccharide chains. The O-antigen 4, 12 specific octasaccharide, covalently linked to different carrier proteins, elicited both in rabbits and mice antibodies with

Single-pipetting microfluidic assay device for rapid detection of Salmonella from poultry package.

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A direct, sensitive, near-real-time, handheld optical immunoassay device was developed to detect Salmonella typhimurium in the naturally occurring liquid from fresh poultry packages (hereafter "chicken matrix"), with just single pipetting of sample (i.e., no filtration, culturing and/or isolation,
We have previously reported that the prophylactic administration of factor(s) from T-cell supernatants derived from Salmonella enteritidis-immune chickens (ILK) have a favorable effect in controlling or eliminating salmonellosis in neonatal poultry. Experimentally, we have used the intraperitoneal

Salmonella enterica serovar Typhi O:1,9,12 polysaccharide-protein conjugate as a diagnostic tool for typhoid fever.

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Serologic tests play an important role in diagnosis of typhoid fever. In an effort to develop a more defined reagent for these tests, purified Salmonella enterica serovar Typhi (ST) O:1,9,12 polysaccharide was conjugated to human serum albumin (HSA), and the conjugate was purified
To date, there has been no employment of a magnetoelastic (ME) biosensor method to detect Salmonella enterica serovar Typhimurium in soil. The ME biosensor method needs to be investigated and modified for its successful performance. The filtration method, cation-exchange resin method, and
Type 1 fimbriae produced by serovars of Salmonella are characterized by their ability to agglutinate guinea pig erythrocytes in the absence of d-mannose but not in its presence. The FimH protein is the adhesin that mediates this reaction; it is distinct from the major fimbrial protei.n (FimA) that
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