Results 181 to 190 of about 71,467 (221)
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Diphtheria Toxin Fusion Proteins
1998Two different approaches have been undertaken to develop targeted biomolecules for therapeutics. The first was the construction of immunotoxins consisting of monoclonal antibodies chemically linked through a disulfide bond to a plant or bacterial toxin or radionuclide.
F M, Foss +4 more
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2000
Abstract Diphtheria toxin (DTX) is a polypeptide of approximately 60 kDa secreted by the bacterium Corynebacterium diphtheriae, a gram-positive nonsporulating rod. Infection with the bacterium in the nasopharynx and subsequent release of toxin into the circulation accounts for the local and systemic manifestations of diphtheria, a ...
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Abstract Diphtheria toxin (DTX) is a polypeptide of approximately 60 kDa secreted by the bacterium Corynebacterium diphtheriae, a gram-positive nonsporulating rod. Infection with the bacterium in the nasopharynx and subsequent release of toxin into the circulation accounts for the local and systemic manifestations of diphtheria, a ...
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The Journal of Immunology, 1929
Abstract The preparation of diphtheria toxins from the time of its discovery by Behring has been repeatedly investigated with the development of many changes in its preparation, but it still presents many difficulties. The urgent need of strong potent toxins for the Ramon flocculation tests for titration of diphtheria antitoxins, and ...
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Abstract The preparation of diphtheria toxins from the time of its discovery by Behring has been repeatedly investigated with the development of many changes in its preparation, but it still presents many difficulties. The urgent need of strong potent toxins for the Ramon flocculation tests for titration of diphtheria antitoxins, and ...
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Diphtheria toxin-receptor interaction: A polyphosphate-insensitive diphtheria toxin-binding domain
Biochemical and Biophysical Research Communications, 1982Abstract Inositol hexaphosphate, and other polyphosphates, inhibit diphtheria toxin-mediated cytotoxicity by binding to the toxin at a highly cationic site called the P site and preventing toxin binding to cell surface receptors. The binding of diphtheria toxin to a solubilized cell surface glycoprotein (150,000 daltons) is also inhibited by these ...
L, Eidels, L L, Ross, D A, Hart
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Iron and Diphtheria Toxin Production
1975The extreme sensitivity of diphtheria toxin production to the iron concentration of the medium was clearly shown by Pappenheimer and Johnson [1]. Iron level of the medium, therefore, has to be carefully controlled whether diphtheria toxin is produced using a surface or a submerged culture.
S V, Gadre, S S, Rao
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Nature, 1968
ULTRACENTRIFUGAL studies have shown that purified diphtheria toxin is a single protein with a molecular weight of 64,500 and an S20, w of 4.2 (ref. 1). In this communication, I report experiments with a sample of toxin that contains the 4.2 S molecule, and an unusual species with a higher sedimentation constant.
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ULTRACENTRIFUGAL studies have shown that purified diphtheria toxin is a single protein with a molecular weight of 64,500 and an S20, w of 4.2 (ref. 1). In this communication, I report experiments with a sample of toxin that contains the 4.2 S molecule, and an unusual species with a higher sedimentation constant.
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The Diphtheria Toxin Structural Gene
1985While there was considerable indirect evidence that toxinogenesis in Corynebacterium diphtheria was related to lysogeny (FREEMAN 1951; FREEMAN AND MORSE 1952; GROMAN 1953 a, b, 1955; GROMAN and EATON 1955; HOLMES and BARKSDALE 1969), it was not until the report of UCHIDA et al.
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Potent Diphtheria Toxin within the Cells of C. diphtheriae
Nature, 1954ALL the exotoxins except diphtheria toxin have been demonstrated within the bacterial cells in a very early stage of culture. So far as diphtheria toxin is concerned, it has been postulated, but never proved, that the exotoxin is formed within the cell.
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