Results 211 to 220 of about 33,592 (266)
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Enzymatic breakdown of tetanus toxin
Biochemical and Biophysical Research Communications, 1974Abstract 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.
T, Helting, O, Zwister
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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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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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Journal of Neuropathology and Experimental Neurology, 1964
When mice are acutely poisoned by either crude or purified tetanus toxin, a marked increase in number and a moderate increase in size of intramitochondrial dense granules occurs. This is most pronounced in skeletal muscle but also may be observed in brain and spinal cord.
SUMNER I. ZACKS, MICHAEL F. SHEFF
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When mice are acutely poisoned by either crude or purified tetanus toxin, a marked increase in number and a moderate increase in size of intramitochondrial dense granules occurs. This is most pronounced in skeletal muscle but also may be observed in brain and spinal cord.
SUMNER I. ZACKS, MICHAEL F. SHEFF
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Molecular Pharmacology of Botulinum Toxin and Tetanus Toxin
Annual Review of Pharmacology and Toxicology, 1986Botulinum toxin is a term that has been used to describe eight different substances designated types A, B, Cb C2, D, E, F, and G. For many years it was assumed that these eight substances acted at the neuromuscular junction to block acetylcholine release. It is now known that this assumption is not entirely correct.
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On the structure of tetanus toxin
Naunyn-Schmiedeberg's Archives of Pharmacology, 1973Previous results from the literature pertaining to the molecular state of tetanus toxin are reported. By use of disc electrophoresis, gel filtration and ultracentrifugation, it is shown in this paper that tetanus toxin is likely to be constituted of subunits.
B, Bizzini, A, Turpin, M, Raynaud
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Synthetic peptide antigens of tetanus toxin
Molecular Immunology, 1994In this study the immunochemical structure of the heavy chain polypeptide from tetanus toxin was studied. Numerous antigenic determinants were identified by probing a set of overlapping peptides derived from the amino acid sequence of tetanus toxin with polyclonal anti-toxoid antibody preparations.
P M, Fischer, M E, Howden
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The chain composition of tetanus toxin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1973Although 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
C J, Craven, D J, Dawson
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[Detoxification of tetanus toxin].
Archiv fur experimentelle Veterinarmedizin, 1979Reported in this paper are experiments conducted to compare formaldehyde, glyoxal, malondialdehyde, succindialdehyde, glutardialdehyde, adipindialdehyde, beta-propiolacton, and pyrocarbonic acid diethylester for their toxifying properties. Tetanus toxin, 1.5 million dlm/ml or 120 binding units, was used.
W, Künzel, C, Meissner
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