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1.
Appl Environ Microbiol ; 49(3): 718-20, 1985 Mar.
Article in English | MEDLINE | ID: mdl-3994374

ABSTRACT

Hemolymph samples obtained from Limulus polyphemus at the time of collection and after a 1-week holding period exhibited a significant increase in bacterial levels. No differences were observed in the ability of amoebocyte lysate, prepared from these same samples, to gel in the presence of lipopolysaccharide.


Subject(s)
Hemolymph/microbiology , Horseshoe Crabs/microbiology , Animals , Limulus Test , Lipopolysaccharides/analysis
2.
Biochem Biophys Res Commun ; 113(2): 611-7, 1983 Jun 15.
Article in English | MEDLINE | ID: mdl-6870875

ABSTRACT

A Staphylococcus aureus-agglutinating lectin, capable of binding to N-acetyl-D-glucosamine, was isolated from the serum of Limulus polyphemus. The monosaccharide alone was incapable of inhibiting bacterial agglutination by this lectin. Quantitative precipitation studies with purified cell wall-derived teichoic acids, either devoid of or containing N-acetyl-D-glucosamine, confirmed the carbohydrate-binding specificity of the lectin and suggested that secondary, non-specific interactions contribute to binding biomolecules containing this sugar. The agglutination pattern with various S. aureus strains having N-acetyl-D-glucosamine-associated teichoic acid, teichoic acid without this sugar, and no teichoic acid indicated that this cell wall component is not the sole binding site for the lectin on intact S. aureus cells. Affinity gel chromatography, using N-acetyl-D-glucosamine-associated teichoic acid as the specific absorbent, has been used to isolate this lectin from Limulus serum.


Subject(s)
Horseshoe Crabs/analysis , Lectins/isolation & purification , Teichoic Acids/analysis , Agglutination Tests , Animals , Arthropod Proteins , Chemical Precipitation , Chromatography, Affinity
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