Results 121 to 130 of about 27,313 (164)
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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

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

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

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

Binding of flavonoids to staphylococcal enterotoxin B

Food and Chemical Toxicology, 2014
Staphylococcal enterotoxins are metabolic products of Staphylococcus aureus that are responsible for the second-most-commonly reported type of food poisoning. Polyphenols are known to interact with proteins to form complexes, the properties of which depend on the structures of both the polyphenols and the protein.
Evgen Benedik   +3 more
openaire   +2 more sources

Guanidination and nitroguanidination of staphylococcal enterotoxin B

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
Guanidination of the free amino groups of staphylococcal enterotoxin B with 3,5-dimethyl-1-guanylpyrazole converted 31-32 of 33 epsilon-amino groups and 30% of the N-terminal residue. This product, although markedly reduced in solubility, suffered no gross change in conformation and retained full biological activity.
L, Spero   +3 more
openaire   +2 more sources

Antigenicity of Formaldehyde-Inactivated Staphylococcal Enterotoxin B

The Journal of Immunology, 1973
Abstract The reactivity toward or ability to stimulate production of antibodies specific for native staphylococcal enterotoxin B (nSEB) demonstrated by formaldehyde-inactivated toxin (fSEB) is directly related to the extent to which SEB is polymerized by aqueous formaldehyde.
J R, Warren, L, Spero, J F, Metzger
openaire   +2 more sources

Staphylococcal Enterotoxin B

Archives of Biochemistry and Biophysics, 1965
M.S. Bergdoll   +4 more
openaire   +1 more source

Integrative oncology: Addressing the global challenges of cancer prevention and treatment

Ca-A Cancer Journal for Clinicians, 2022
Jun J Mao,, Msce   +2 more
exaly  

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