نتایج جستجو برای: staphylococcal enterotoxin c

تعداد نتایج: 1087222  

Journal: :Infection and immunity 1975
L Spero D L Leatherman W H Adler

Staphylococcal enterotoxin B is a potent mitogen for mouse and human lymphocytes. Mitogenic activity was retained after detoxification of the enterotoxin by formaldehyde at pH 5.0, 7.5, OR 9.5. The most active toxoid (pH 7.5) was separated into a monomeric, a dimeric, and a polymeric fraction (1 x 10(5) to 3 x 10(5) molecular weight) by gel filtration, and although each fraction demonstrated mi...

ژورنال: Anatomical Sciences Journal 2009
Imani Fouladi, Abbas Ali, Nourani , Mohammad Reza,

Purpose: Staphylococcal enterotoxin B (SEB) is a potent inducer of cytotoxic T-cell activity, cytokine production and necrosis induction in vivo. Monophosphoryl lipid A (MPL) is an adjuvant derived from the lipopolysaccharide of E.coli, Salmonella Minnesota Re595 and other gram negative bacteria.Materials and Methods: In this research, The antitumor and antimetastatic effect of intra-venus inje...

Journal: :Euro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin 2010
A Ostyn M L De Buyser F Guillier J Groult B Felix S Salah G Delmas J A Hennekinne

At the end of 2009, six food poisoning outbreaks caused by staphylococci were reported in France. Soft cheese made from unpasteurized milk was found to be the common source of the outbreaks. Staphylococcal enterotoxin type E was identified and quantified in the cheese using both official and confirmatory methods of the European Union Reference Laboratory (EU-RL). To our knowledge, this is the f...

Journal: :Applied and environmental microbiology 1988
L Bautista P Gaya M Medina M Nuñez

Of 124 staphylococcal strains isolated from sheep milk, 78 produced enterotoxin A, B, C, or D when evaluated by an enzyme-linked immunosorbent assay. Enterotoxins A and D, elaborated by 44 and 43 strains, respectively, showed the highest incidence. Enterotoxin production by coagulase-negative strains (one Staphylococcus cohnii, three S. epidermidis, five S. haemolyticus, and four S. xylosus) wa...

Journal: :Journal of clinical microbiology 1979
B M Brill B L Wasilauskas S H Richardson

Protein A-containing staphylococci coated with specific antiserum were tested for heat-labile enterotoxin of Escherichia coli. The immunological cross-reactivity of E. coli heat-labile enterotoxin with Vibrio cholerae toxin (choleragen) was the basis for sensitizing stabilized suspensions of the Cowan I strain of Staphylococcus aureus with anticholeragen. Unconcentrated culture supernatant flui...

Journal: :Applied microbiology 1975
J Y Humber C B Denny C W Bohrer

The effect of pH on the thermal inactivation of staphylococcal enterotoxin A was investigated. Analysis of heated toxin by immunodiffusion in gel indicated that enterotoxin A in beef bouillon was inactivated faster at pH 5.3 than at pH 6.2. The z values (slopes) for the heat inactivation curves at pH 6.2 and 5.3 were 49.5 and 55 F (about 27 and 30 C), respectively. Enterotoxin produced and heat...

Journal: :Microbiology resource announcements 2021

We report a de novo -assembled draft genome sequence of the Indian Staphylococcus aureus type 88 (ST88) strain LVP-7, isolated from an ocular infection. The harbors Panton-Valentine leukocidin phage, V staphylococcal cassette chromosome mec element, delta-hemolysin-converting Newman phage ΦNM3, and pathogenicity island SaPI3, encoding superantigen enterotoxin B.

Journal: :Applied and environmental microbiology 1983
I A Ende G Terplan B Kickhöfen D K Hammer

A new chromatographic procedure was developed which obtained highly purified preparations of staphylococcal enterotoxins B and C1 in yields of 60% from cultures of Staphylococcus aureus and which is faster than any of the separation methods used previously. The procedure involves chromatography on carboxymethylcellulose, removal of alpha-toxin by adsorption to rabbit erythrocyte membranes, and ...

2003
LEONARD SPERO

The in vitro exposure of staphylococcal enterotoxin B to trypsin resulted in the formation within 30 min of a product (enterotoxin-T) unchanged in molecular weight, but with threonine as a second NH2 terminus. Upon reduction of the -SSbridge in enterotoxin-T, two fragments were separated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The peptide bond between Lys-97 and Thr-98 ...

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