Interaction of fragment A from diphtheria toxin with nicotinamide adenine dinucleotide.
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Animals↗
Biomedical subjects
R J Collier
Publications and source records attributed to R J Collier.
Interaction of transferase II with polynucleotides and inhibition of the interaction by guanosine nucleotides.
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Adenosine Diphosphate↗
Structure and activity of diphtheria toxin. I. Thiol-dependent dissociation of a fraction of toxin into enzymically active and inactive fragments.
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Acrylates↗
Structure and activity of diphtheria toxin. II. Attack by trypsin at a specific site within the intact toxin molecule.
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Acrylates↗
Binding of transfer factor II to ribosomal RNA and inhibition of the binding by guanosine nucleotides.
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Adenine Nucleotides↗
Diphtheria toxin subunit active in vitro.
Exposure of diphtheria toxin to dithiothreitol (and similar thiols) resulted in a subunit which was active in catalyzing the adenosine diphosphateribosylation of mammalian aminoacyl-transferase II in the presence of nicotinamide adenine dinucleotide. At the same time there was a marked increase in total ADP-ribosylation activity. A molecule which was apparently identical to the derived subunit in size and activity was detected in partially purified preparations of toxin.
Adenine Nucleotides↗
Inactivation of aminoacyl transferase II by diphtheria toxin.
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Acyltransferases↗
An X-band electron spin resonance spectrometer with a ruby maser preamplifier.
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Electron Spin Resonance Spectroscopy↗
Effect of diphtheria toxin on protein synthesis: inactivation of one of the transfer factors.
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Amino Acids↗
Differences in the immunogenicity of native and formalinized cross reacting material (CRM197) of diphtheria toxin in mice and guinea pigs and their implications on the development and control of diphtheria vaccine based on CRMs.
Immunogenicity of native and formalinized cross reacting material (CRM197) of diphtheria toxin (DTx) was assessed in mice and guinea pigs. For the primary response, mice produced similar levels of diphtheria toxoid (DTxd) IgG antibodies to both native and formalinized preparations of CRM197 though the antibody levels were significantly lower than those elicited by conventional DTxd (P < 0.05). In contrast, guinea pigs showed significantly higher levels of DTxd IgG antibodies to the formalinized CRM197 preparation than the native preparation (P < 0.001) after single injection. These differences in the immunogenicity of mice and guinea pigs to native and formalinized CRM197 preparations have implications for the development and control of diphtheria or other vaccines involving the use of CRMs.
Animals↗