Results 181 to 190 of about 13,773,627 (236)
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Raising Antibodies to Staphylococcal Enterotoxins A and B

Journal of Applied Bacteriology, 1977
A method is described for raising specific antibodies to staphylococcal enterotoxins A (SEA) and B (SEB) by intravenous inoculation of rabbits with small doses of enterotoxin diluted in sterile physiological saline. A course of six injections over a period of two weeks was given on four occasions.
C M, Bradstreet   +3 more
openaire   +2 more sources

A staphylococcal enterotoxin B magnetoelastic immunosensor

Biosensors and Bioelectronics, 2004
A magnetoelastic immunosensor for detection of staphylococcal enterotoxin B (SEB) is described. The magnetoelastic sensor is a newly developed mass/elasticity-based transducer of high sensitivity having a material cost of approximately $0.001/sensor.
Chuanmin, Ruan   +3 more
openaire   +2 more sources

Immunosuppression induced by staphylococcal enterotoxin B

Cellular Immunology, 1982
Abstract Staphylococcal enterotoxin B (SEB) is a potent mitogen for both human and murine T lymphocytes. We report here studies which demonstrate that a suppressor cell population, capable of suppressing the primary immune response of normal syngeneic mouse splenocytes to heterologous sheep erythrocytes (SRBC), is activated by SEB.
Donnelly, R P, Rogers, T J
openaire   +2 more sources

Microheterogeneity of staphylococcal enterotoxin B

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1974
Abstract Four components have been demonstrated in staphylococcal enterotoxin B by isoelectric focusing in polyacrylamide gels. In a typical preparation their relative concentrations from the most to least cathodic were 6, 56, 31 and 7%. The components were not stable conformers nor were the differences in isoionic points due to bound ligand.
Leonard Spero   +2 more
openaire   +1 more source

Staphylococcal Enterotoxin B

2003
Toxins are biologically derived substances that adversely affect living organisms. An astounding number of toxins produced by animals, plants, and bacteria are harmful to humans. Toxins cause food poisonings and envenomations, bleeding disorders, and neurological dysfunction.
openaire   +1 more source

Crystal structure of staphylococcal enterotoxin B, a superantigen

Nature, 1992
The three-dimensional structure of staphylococcal enterotoxin B, which is both a toxin and a super-antigen, has been determined to a resolution of 2.5 A. The unusual main-chain fold containing two domains may represent a general motif adopted by all staphylococcal enterotoxins.
S, Swaminathan   +3 more
openaire   +2 more sources

Hydroxyl apatite column chromatography of enterotoxin B

Canadian Journal of Microbiology, 1971
Purified enterotoxin B was resolved into three components by hydroxyl apatite column chromatography. Only one of these components was toxic, but all three appeared to be serologically identical.
P C, Chang, N, Dickie, F S, Thatcher
openaire   +2 more sources

The secondary structure of staphylococcal enterotoxins A, B and C

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1980
The circular dichroism (CD) of staphylococcal enterotoxins A, B and C was measured. The CD of enterotoxins B and C were almost identical from 250 to 320 nm, but differed from the CD of enterotoxin A. The spectrum of enterotoxin A in this wavelength region contained the same bands with respect to both location and sign, but with significant differences ...
J L, Middlebrook, L, Spero, P, Argos
openaire   +2 more sources

The mitogenic effects of endotoxin and staphylococcal enterotoxin B on mouse spleen cells and human peripheral lymphocytes.

Journal of Immunology, 1970
The effects of Salmonella endotoxin and staphylococcal enterotoxin B (SEB) were examined in vitro on mouse and human lymphocyte populations from unsensitized subjects.
D. L. Peavy   +2 more
semanticscholar   +1 more source

On the Cross-Reactivity of Staphylococcal Enterotoxins A, B, and C

The Journal of Immunology, 1978
Abstract Strong cross-reactions were demonstrated for staphylococcal enterotoxins B (SEB) and C1 (SEC1) by antigenbinding capacity and by competitive binding ability. Both SEB and SEC1 combined completely with the heterologous antibody although requiring four times as much antiserum as the homologous enterotoxin and both displaced about ...
L, Spero, B A, Morlock, J F, Metzger
openaire   +2 more sources

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