Results 171 to 180 of about 12,387,393 (211)
Some of the next articles are maybe not open access.
Regulation of Staphylococcal Enterotoxin B
Journal of Bacteriology, 1969Several factors influenced the formation of enterotoxin B by Staphylococcus aureus strain S-6. In the standard casein hydrolysate medium, toxin was not produced in detectable quantities during exponential growth; it was produced during the post-exponential phase when total protein synthesis was arithmetic.
S A, Morse, R A, Mah, W J, Dobrogosz
openaire +2 more sources
Heterogeneity of staphylococcal enterotoxin B
Canadian Journal of Microbiology, 1971Different forms of enterotoxin B obtained by hydroxyl apatite column chromatography and isoelectric focusing were found to produce lines of apparent serologic identity, but to differ in toxicity. This is interpreted to mean that the antigenic site or sites and toxic site or sites are most probably not the same in the molecule of enterotoxin B.
P C, Chang, N, Dickie
openaire +2 more sources
Fractions of Staphylococcal Enterotoxin B
Nature, 1965IN a recent paper1 we showed that enterotoxin B isolated from Staphylococcus aureus strain S6 could be separated into two main protein fractions by starch-gel electrophoresis. After the completion of this work we received communications concerning this observation from Dr. M. S. Bergdoll (University of Chicago) and from Dr. E. J. Schantz (U.S.
R L, Joseph, A C, Baird-Parker
openaire +2 more sources
Raising Antibodies to Staphylococcal Enterotoxins A and B
Journal of Applied Bacteriology, 1977A 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
Guanidination and nitroguanidination of staphylococcal enterotoxin B
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971Guanidination 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
Binding of flavonoids to staphylococcal enterotoxin B
Food and Chemical Toxicology, 2014Staphylococcal 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
Immunosuppression induced by staphylococcal enterotoxin B
Cellular Immunology, 1982Abstract 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, 1974Abstract 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
The secondary structure of staphylococcal enterotoxins A, B and C
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1980The 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
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
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