Purification, Properties and Amino Acid Sequence of α-Bungarotoxin from the Venom of<i>Bungarus multicinctus</i>

Mebs, Dietrich; Narita, Kozo; Iwanaga, Sadaaki; Samejima, Yuji; Lee, Chen-Yuan

doi:10.1515/bchm2.1972.353.1.243

Cited by 159 publications

(37 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Bovine trypsin (three times crystallized) was from Worthington Bie chemicals Corp. a-Bungarotoxin was a preparation made by Dr. D. Mebs, Frankfurt (Germany) [3]. Purified bovine plasma kalllkrein [4] and bovine plasmin [5] were prepared by the methods reported previously.…”

Section: Methodsmentioning

confidence: 99%

Isolation of a novel inhibitor of kallikrein, plasmin and trypsin from the venom of russell's viper (Vipera russelli)

1972

Self Cite

View full text Add to dashboard Cite

Section: Methodsmentioning

confidence: 99%

Isolation of a novel inhibitor of kallikrein, plasmin and trypsin from the venom of russell's viper (Vipera russelli)

1972

Self Cite

View full text Add to dashboard Cite

“…x-Bungarotoxin and toxin B were isolated and purified from the venom of Bungavus rnulticinctus [20] and Naju naju …”

Section: Mutevialsmentioning

confidence: 99%

“…However, appreciable differences in the affinity to acetylcholine receptor [14,15] and in the effect of chemical modifications [16-181 have been found between the groups of short and long neurotoxins. Accordingly, it is of interest to compare the solution structures of long neurotoxins with those of short neurotoxins and to elucidate the common structural characteristics responsible for neurotoxicity.a-Bungarotoxin and toxin B are long neurotoxins isolated from the venom of Bungarus rnulticinctus and Naja nuja, respectively (see Table 1 for the primary structures) [6,[19][20][21]. x-Bungarotoxin is widely used for assaying the acetylcholine receptor protein antibody because of its potent -Ahhrc4ation.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Proton‐Nuclear‐Magnetic‐Resonance Study on Molecular Conformations of Long Neurotoxins

Endo

Inagaki

Hayashi

et al. 1981

European Journal of Biochemistry

View full text Add to dashboard Cite

The 270-MHz proton N M R spectra were analyzed of tlie long neurotoxins a-bungarotoxin from Bungcrru.~ nzulzicincius and Toxin B from Nuju nuju. The aromatic proton resonances were completely assigned to individual nuclei for a-bungarotoxin and in part for toxin B. The pH dependences of proton chemical shifts were analyzed by the nonlinear least-square method, for obtaining pK, values and protonation shifts. The pK, values of Tyr-25, an invariant residue of neurotoxins, are 12.1 for x-bungarotoxin and 11.3 for toxin B, suggesting the presence of a strong hydrogen bond involving Tyr-25 in a-bungarotoxin. The Trp-29 residues of both toxins show a common titration shift due to the carboxylate group of Asp-31 and a similar structural arrangement of functionally invariant pair of Trp-29 and Asp-31 is implied. From the temperature dependences of the chemical shifts of His-68 and a methyl group of x-bungarotoxin, the local structure around His-68 near the tail part is shown to be more flexible than the other part. The six main-chain amide protons of a-bungarotoxin exchange most slowly with solvent deuterons and are found by interproton nuclear Overhauser effects to be in the /]-sheet near the aromatic ring of Tyr-25 residue. Hydrogen --$ deuterium exchange rates in 2 H 2 0 solution at 37 "C were measured of slowly exchanging amide protons of 3-bungarotoxin, toxin B, and two short neurotoxins, namely cobrotoxin and erabutoxin b. The two long neurotoxins have amide protons with relatively long half-times spanning as long as 10-100 h, but the two short neurotoxins do not have amide protons with half-times longer than 3 h. The distributions of the half-times of amide proton exchange indicate the structural rigidity of neurotoxins in the order, Neurotoxic proteins from the venom of Hydrophid and Elapid snakes block the neuromuscular transmission at the post-synaptic level by the specific binding to the acetylcholine receptor protein [I]. They are classified into two groups, short neurotoxins with 60-62 amino acid residues and long neurotoxins with 71 -74 residues. The three-dimensional structures in crystals have been elucidated of both types of neurotoxins, iximi.1) erabutoxin b from Luricaudu sern(fusciuzu [2-51 and x-cobratoxin from Nuja naju siumensis [6]. The solution. structures have been investigated more intensively for short neurotoxins than for long neurotoxins by physico-chemical methods including nuclear magnetic resonance (NMR) spectroscopy [7 -131. However, appreciable differences in the affinity to acetylcholine receptor [14,15] and in the effect of chemical modifications [16-181 have been found between the groups of short and long neurotoxins. Accordingly, it is of interest to compare the solution structures of long neurotoxins with those of short neurotoxins and to elucidate the common structural characteristics responsible for neurotoxicity.a-Bungarotoxin and toxin B are long neurotoxins isolated from the venom of Bungarus rnulticinctus and Naja nuja, respectively (see Table 1 for the primary structures) [...

show abstract

“…Neutralization of NT-I in a mouse lethal assay was not attempted because of the high LD50 (560 ,ug/kg; Grishin et al, 1974), in contrast with a-BT (150 ,tg/kg; Mebs et al, 1972), and difficulty in obtaining favourable NT-i mAb molar ratios.…”

Section: Inhibition Of X-bt Binding To Achr In Vitro By Nt-1 Mabsmentioning

confidence: 99%

Characterization of monoclonal antibodies against Naja naja oxiana neurotoxin I

Stiles

Sexton

Guest

et al. 1994

Biochemical Journal

View full text Add to dashboard Cite

Seven monoclonal antibodies (mAbs) were developed against neurotoxin I (NT-1), a protein from central Asian cobra (Naja naja oxiana) venom which binds specifically to nicotinic acetylcholine receptor (AchR). All of the mAbs cross-reacted with another long-chain post-synaptic neurotoxin, Bungarus multicinctus alpha-bungarotoxin (alpha-BT), but not Naja naja kaouthia alpha-cobratoxin, in an enzyme-linked immunosorbent assay (e.l.i.s.a.). Short-chain post-synaptic neurotoxins like Naja naja atra cobrotoxin, Laticauda semifasciata erabutoxin b, or N. n. oxiana neurotoxin II did not cross-react with the NT-1 mAbs, but an antigen(s) found in Dendroaspis polylepis, Acanthophis antarcticus and Pseudechis australis venoms was immunoreactive. The e.l.i.s.a. readings for dithiothreitol-reduced NT-1 and NT-1 mAbs ranged from 13 to 27% of those for native toxin but reduced alpha-BT was not immunoreactive. Synthetic NT-1 peptides were used in epitope-mapping studies and two, non-contiguous regions (Cys15-Tyr23 and Lys25-Gly33 or Pro17-Lys25 and Asp29-Lys37) were recognized by the NT-1 mAbs. The NT-1 mAbs individually inhibited 31-71% of alpha-BT binding to AchR in vitro and afforded a slight protective effect in vivo with a toxin: antibody mole ratio of 1:1.5. This report is the first to describe mAbs which recognize and protect against a heterologous, long-chain, post-synaptic neurotoxin from snake venom.

show abstract

Purification, Properties and Amino Acid Sequence of α-Bungarotoxin from the Venom ofBungarus multicinctus

Cited by 159 publications

References 0 publications

Isolation of a novel inhibitor of kallikrein, plasmin and trypsin from the venom of russell's viper (Vipera russelli)

Isolation of a novel inhibitor of kallikrein, plasmin and trypsin from the venom of russell's viper (Vipera russelli)

Proton‐Nuclear‐Magnetic‐Resonance Study on Molecular Conformations of Long Neurotoxins

Characterization of monoclonal antibodies against Naja naja oxiana neurotoxin I

Contact Info

Product

Resources

About