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[Staphylococcal enterotoxin. I. Production of enterotoxin B in various media].

Roczniki Panstwowego Zakladu Higieny, 1969
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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, Mihaela Skrt, Črtomir Podlipnik, Nataša Poklar Ulrih   +3 more
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Methicillin-resistant Staphylococcus aureus (MRSA) isolated from chicken meat and giblets often produces staphylococcal enterotoxin B (SEB) in non-refrigerated raw chicken livers.

Journal of food microbiology, 2020
Methicillin-resistant Staphylococcus aureus (MRSA) is responsible for several difficult-to-treat infections and staphylococcal food poisoning (SFP). This study was conducted to investigate the prevalence and enterotoxigenicity of MRSA in broiler chicken ...
S. Abolghait, Amal Gamal Fathi, F. Youssef, A. Algammal   +3 more
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Nanobodies Based on a Sandwich Immunoassay for the Detection of Staphylococcal Enterotoxin B Free from Interference by Protein A.

Journal of Agricultural and Food Chemistry, 2020
Being one of the leading causes of food poisoning, Staphylococcal enterotoxins (SEs) secreted by Staphylococcus aureus (S.aureus), pose a serious threat to human health. The immunoassay has become the dominant tool used for the rapid detection of harmful
Yanwei Ji, Xiang Li, Yunlong Lu, Peng Guo, Ganwei Zhang, Yanru Wang, Yi Zhang, Wenxin Zhu, Jiachuan Pan, Jianlong Wang   +9 more
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Development of sandwich chemiluminescent immunoassay based on an anti-staphylococcal enterotoxin B Nanobody-Alkaline phosphatase fusion protein for detection of staphylococcal enterotoxin B.

Analytica Chimica Acta, 2020
In this study, sandwich chemiluminescent immunoassay (CLIA) for the detection of Staphylococcal enterotoxin B (SEB) was developed using nanobody-alkaline phosphatase (Nb-ALP) fusion protein.
Tieqiang Sun, Zunquan Zhao, Wentao Liu, Zehua Xu, Hongwei He, Baoan Ning, Yongqiang Jiang, Zhixian Gao   +7 more
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Silver nanoparticle-base lateral flow immunoassay for rapid detection of Staphylococcal enterotoxin B in milk and honey.

Journal of Inorganic Biochemistry, 2020
A silver nanoparticle (AgNP)-based sandwich-type lateral flow immunoassay (LFIA) was evaluated for rapid detection of Staphylococcal enterotoxin B (SEB) in milk and honey.
Kuo-Hui Wu, Wen-Chien Huang, Rong-Hwa Shyu, Shu-Chen Chang   +3 more
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Regulation of Staphylococcal Enterotoxin B

Journal of Bacteriology, 1969
Several 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
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Fractions of Staphylococcal Enterotoxin B

Nature, 1965
IN 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
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Heterogeneity of staphylococcal enterotoxin B

Canadian Journal of Microbiology, 1971
Different 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
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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, H M, Jacoby, J E, Dalidowicz, S J, Silverman   +3 more
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