Results 211 to 220 of about 318,498 (273)
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On the similarity of tetanus and botulinum toxins

Naunyn-Schmiedeberg's Archives of Pharmacology, 1973
1. Botulinum toxin blocks neuromuscular transmission to the abductor superficialis muscle of the goldfish pectoral fin. Since the botulinum-paralysed muscles are still responsive to direct electrical stimulation and to carbachol it is probable that the toxin acts (at least partly) presynaptically.
Nicola Hampden   +2 more
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Purification of tetanus toxin

Biochimica et Biophysica Acta, 1956
Abstract The combination of multi-membrane electro-decantation and ammonium sulphate fractionation resulted in an effective purification of tetanus toxin. The most highly purified material obtained in this way contained as much as 4300–4800 Lf per mg protein nitrogen.
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The chain composition of tetanus toxin

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1973
Although tetanus toxins from cell and culture filtrate appear indistinguishable by several criteria, only the filtrate toxin can be cleaved into two chains by disulfide scission. These chains approximate molecular weights of 95,000 and 55,000. Determinations of sulfhydryl groups and total half-cystine residues for both the cell and filtrate toxins gave
Cyril J. Craven, Desmond J. Dawson
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Mode of Action of Tetanus Toxin [PDF]

open access: possibleNature, 1955
THOUGH the general effects produced by tetanus toxin on the nervous system have been reported by many investigators, there is still no precise evidence as to its mode of action1. Sherrington2 pointed out that tetanus toxin closely resembles strychnine in many of its effects, and postulated that both substances convert synaptic inhibition into ...
V. B. Brooks   +2 more
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Tetanus toxin and spinal inhibition

Brain Research, 1968
Summary Tetanus toxin blocks the synaptic inhibition of feline Renshaw cells elicited by hind paw stimulation without affecting the inhibitory action of electrophoretically administered glycine. Assuming that glycine is the transmitter at spinal inhibitory synapses, these results indicate that tetanus toxin blocks the inhibitory process by reducing ...
David R. Curtis, W. C. De Groat
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Enzymatic breakdown of tetanus toxin

Biochemical and Biophysical Research Communications, 1974
Abstract Treatment of tetanus toxin with papain at 55°C resulted in breakdown of the molecule to yield an atoxic fraction with a molecular weight of approximately 40 000. The highly purified material exhibited partial immunological identity with the parent toxin, showed no toxicity and elicited the formation of neutralizing antibodies against tetanus.
Oswald Zwisler, Torsten Helting
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On the similarity of tetanus and cholera toxins

Naunyn-Schmiedeberg's Archives of Pharmacology, 1973
There are several similarities between tetanus and cholera toxins, including their ability to react with ganglioside. However, tetanus toxin reacts mostly with certain gangliosides containing sialidase-sensitive bonds, whereas cholera toxin reacts only with one particular ganglioside that does not contain any sialidase-sensitive bonds.
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The flocculation of tetanus toxin and toxoid. I

Antonie van Leeuwenhoek, 1954
1. The flocculation of tetanus toxins and toxoids produced in a modified Tarozzi broth was made the subject of an exhaustive study. 2. At least three flocculation zones were found. 3. The lowest flocculation value always proved to agree with the true point of equivalence of the antitoxin-binding (A.B.V.). 4.
H. Rijks, J. D. van Ramshorst
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Studies on tetanus toxin

Biochimica et Biophysica Acta (BBA) - General Subjects, 1965
Abstract A new method for the preparation of highly purified tetanus by column chromatography is described. The product was characterised by electrophoretic and immunoelectrophoretic techniques. Fluorescent labels were attached to the toxin without altering its electrophoretic properties or toxicity.
M.B. Perry, S. I. Zacks, M. F. Sheff
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The transglutaminase hypothesis for the action of tetanus toxin

Trends in Biochemical Sciences, 1993
Tetanus toxin potently and almost irreversibly inhibits the release of neurotransmitters from nerve terminals. The toxin binds to and activates transglutaminase, a Ca(2+)-dependent enzyme that can form stable crosslinks between substrate proteins. Transglutaminase is present in nerve terminals and recognizes synapsin I, an abundant synaptic vesicle ...
F. FACCHIANO   +3 more
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