Interaction of an Endotoxin with Cationic Macromolecules

Mora, Peter T.; Young, Bobby G.

doi:10.1099/00221287-26-1-81

Cited by 14 publications

(3 citation statements)

References 16 publications

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“…The main portion of the turbidimetrically measured interaction is thus similar to the electrostatic interactions previously observed between cationic macromolecules and endotoxins (Mora and Young, 1961;Oroszlan, Mora, and Shear, 1963;Rudbach and Johnson, 1964) and in all probability is not the colicine-enhancing mechanism. It is also evident that the electrostatic complex formation does not serve as an initial starting point from which the colicine activation mechanism can work, since native hemoglobin is effective without such a platform.…”

Section: Resultssupporting

confidence: 77%

Turbidimetric Changes Accompanying the Interaction of Endotoxin and the α Chains of Human Hemoglobin

1965

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SETLOW, PETER (Brandeis University, Waltham, Mass.), LAWRENCE LEVINE, AND HELEN VAN VUNAKIS. Turbidimetric changes accompanying the interaction of endotoxin and the a chains of human hemoglobin. J. Bacteriol. 89:1237-1243. 1965.-With the use of a turbidimetric assay, the effects of pH, ionic strength, anions and cations, and varying concentrations of reactants on the interaction of Escherichia coli endotoxin (prepared by the Boivin procedure) with the a chain of hemoglobin were studied. The reaction was found to be partially reversible by addition of NaCl or by addition of an excess of either reactant. The characteristics of the reaction indicated that complex formation between two multivalent molecules had taken place. The formation of the complex was inhibited by endotoxin (prepared by the Westphal procedure) and by the products which resulted from partial tryptic digestion of a chain.

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Section: Resultssupporting

confidence: 77%

Turbidimetric Changes Accompanying the Interaction of Endotoxin and the α Chains of Human Hemoglobin

1965

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“…Nevertheless, it is the same order of magnitude as in other mammalian receptors-e.g., oPRL receptors in the rat mammary gland (17) and FSH receptors in the rat testis (18). The competition experiments with unlabeled hCG and other hormones suggest that binding of gonadotropin to P. maltophilia is not simply an ionic interaction between cationic ligands and the anionic lipopolysaccharide complex of the bacterial outer membrane (19). The hormones that show maximal binding, hCG and hLH, have isoelectric points of 3.0(20) and 5.4 (21), respectively.…”

Section: Methodsmentioning

confidence: 98%

Specific gonadotropin binding to Pseudomonas maltophilia.

Richert¹,

Ryan²

1977

Proc. Natl. Acad. Sci. U.S.A.

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Binding of 1251-labeled human chorionic gonadotropin to Pseudomonas maltophifia is dependent on time, temperature, and pH and the binding to this procaryotic species is hormone-specific and saturable. The equilibrium dissociation constant is 2.3 X 10-9 M. There are no cooperative interactions between binding sites (Hill coefficient, 1.05 Stock cultures were maintained on eosin-methylene blue agar plates and nutrient agar slants at room temperature. For binding studies, several small (1-2 mm) granular colonies were inoculated into a sterile tube containing 5 ml of trypticase soy broth, pH 7.4. After overnight incubation at 300 in a shaking water bath, the culture was transferred to a 2-liter sterile flask containing 500 ml of trypticase soy broth and grown to stationary phase at 30°in a shaking water bath (100 oscillations/ min).* Stationary phase cultures had an optical density (turbidity) at 625 nm of 3.5-9.0, depending on the bacterial strain. Although binding activity was tested twice a day during all phases of growth, maximal binding in P. maltophilia generally occurred within 48 hr after the culture reached stationary phase.Preparation of Bacterial Pellets for Binding Assays. Bacteria were harvested by centrifugation at 20,000 X g for 20 min at 40 and washed twice with an equivalent volume of 40 mM Tris-HCl, pH 7.4. The pellets were resuspended at a 10-fold concentration in 40 mM Tris-HCl, pH 7.4, containing 10% sucrose. These pellets could be stored at -700 for 6 months without appreciable loss of binding activity. For

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“…The evidence is accumulating that complex formation between endotoxins and various proteins can alter the biological and serological properties of endotoxins. The ability of strong cationic macromolecules and proteins to inactivate the tumor-necrotizing activity of S. marcescens endotoxin could be reversed by treating the complexes with the polyanion, polyglucose sulfate (26,27). Using proteolytic enzyme digestion, Rudbach and Johnson (28) have also been able to restore pyrogenic and immunological activities to S. typhosa endotoxin previously rendered inactive by treatment with Cohn fraction IV-1.…”

Section: Discussionmentioning

confidence: 99%

Enhancement of Antibiotic Activity of Colicine K and Alteration of Serological Properties of Colicine K and Endotoxins

Vunakis

Ruffilli

Levine

1965

The Journal of Experimental Medicine

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Hemoglobin, its chains, and myoglobin enhance the antibiotic activity of colicine K. These proteins also interact with colicine K and other O antigens to alter their serological activity. The hemoglobin proteins did not alter the serological activities of three Pneumococcus polysaccharides or T4 bacteriophage DNA antigens but did alter the antigenic activity of fetuin. Interaction of hemoglobin and colicine K resulted in a retardation of colicine K antibiotic moiety as measured by gel filtration but did not affect the gel filtration properties of the lipopolysaccharide moiety.

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Interaction of an Endotoxin with Cationic Macromolecules

Cited by 14 publications

References 16 publications

Turbidimetric Changes Accompanying the Interaction of Endotoxin and the α Chains of Human Hemoglobin

Turbidimetric Changes Accompanying the Interaction of Endotoxin and the α Chains of Human Hemoglobin

Specific gonadotropin binding to Pseudomonas maltophilia.

Enhancement of Antibiotic Activity of Colicine K and Alteration of Serological Properties of Colicine K and Endotoxins

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