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Purification of a Lethal Toxin of Edwardsiella tarda

open access: yesPurification of a Lethal Toxin of Edwardsiella tarda
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β-Cyclodextrin derivatives that inhibit anthrax lethal toxin

Bioorganic and Medicinal Chemistry, 2006
Recently, we demonstrated that simultaneous blocking of bacterial growth by antibiotics and inhibition of anthrax toxin action with antibodies against protective antigen were beneficial for the treatment of anthrax. The present study examined the hypothesis that blocking the pore formed by protective antigen can inhibit the action of anthrax toxin. The
Nour Eddine Fahmi   +2 more
exaly   +3 more sources

Validation of the anthrax lethal toxin neutralization assay

Biologicals, 2004
A validation of the performance characteristics of a toxin neutralization assay is presented. This in vitro assay measures the functional ability of antisera, containing antibodies to anthrax lethal toxin, to specifically protect J774A.1 cells against Bacillus anthracis lethal toxin cytotoxicity.
Donna, Hering   +5 more
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Disulfide Bonds of Purothionin, a Lethal Toxin for Yeasts

The Journal of Biochemistry, 1978
Purothionin isolated from commercial wheat flour contained several components and two of them (A-I and A-II) were isolated in pure form by CM-52 column chromatography. Each component contained 45 amino acid residues with a 4 disulfide bonds. Purothionin A-II was digested with trypsin and thermolysin to isolate cystine peptides. These were separated and
T, Hase, H, Matsubara, H, Yoshizumi
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Purification of a lethal toxin produced by Shigella dysenteriae

Toxicon, 1982
A lethal toxin was purified from the culture supernatant of Shigella dysenteriae 1. The purification procedure utilized ammonium sulfate fractionation, column chromatography on DEAE-cellulose, CM-cellulose, hydroxylapatite and gel filtration on Sephadex G-200. About a 4760-fold purification was achieved, with a yield of 2.7%.
K, Okamoto, Y, Takeda, T, Miwatani
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Anthrax lethal toxin: a weapon of multisystem destruction

Cellular and Molecular Life Sciences, 2004
Lethal toxin (LT) is a major virulence factor secreted by anthrax bacteria. It is composed of two proteins, PA (protective antigen) and LF (lethal factor). PA transports the LF inside the cell, where LF, a zinc-dependent metalloprotease cleaves the mitogen activated protein kinase kinase (MAPKK) enzymes of the mitogen activated protein kinase (MAPK ...
A, Agrawal, B, Pulendran
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The Pathogenesis of the Lethal Effect of Anthrax Toxin in the Rat

Journal of Infectious Diseases, 1966
ditions previously described (Beall et al, 1962). After 24 hours growth the bulk of the bacteria was removed by centrifugation, and the crude or unfractionated toxin used in these experiments was prepared in 1 of 2 ways: (a) the culture was sterilized by filtration through Millipore filters in stainless steel funnels, frozen, and stored at ?20 C; or (b)
F A, Beall, F G, Dalldorf
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Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity

Molecular Microbiology, 1994
SummaryComparison of the anthrax toxin lethal factor (LF) amino acid sequence with sequences in the Swiss protein database revealed short regions of similarity with the consensus zinc‐binding site, HEXXH, that is characteristic of metalloproteases. Several protease inhibitors, including bestatin and captopril, prevented intoxication of macrophages by ...
K R, Klimpel, N, Arora, S H, Leppla
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