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ChemicalBook--->CAS DataBase List--->142948-19-4

142948-19-4

142948-19-4 Structure

142948-19-4 Structure
IdentificationBack Directory
[Name]

LEIUROTOXIN I
[CAS]

142948-19-4
[Synonyms]

LETX I
SCYLLATOXIN
LEIUROTOXIN I
Scyllatoxin, LeTx I
LETX I SCORPION TOXIN
Leiurotoxin I Scyllatoxin, LeTx I
SCYLLATOXIN (SCORPION, LEIURUS QUINQUESTRIATUS HEBRAEUS)
LEIUROTOXIN I (SCORPION, LEIURUS QUINQUESTRIATUS HEBRAEUS)
ALA-PHE-CYS-ASN-LEU-ARG-MET-CYS-GLN-LEU-SER-CYS-ARG-SER-LEU-GLY-LEU-LEU-GLY-LYS-CYS-ILE-GLY-ASP-LYS-CYS-GLU-CYS-VAL-LYS-HIS-NH2
H-ALA-PHE-CYS-ASN-LEU-ARG-MET-CYS-GLN-LEU-SER-CYS-ARG-SER-LEU-GLY-LEU-LEU-GLY-LYS-CYS-ILE-GLY-ASP-LYS-CYS-GLU-CYS-VAL-LYS-HIS-NH2
H-ALA-PHE-CYS-ASN-LEU-ARG-MET-CYS-GLN-LEU-SER-CYS-ARG-SER-LEU-GLY-LEU-LEU-GLY-LYS-CYS-ILE-GLY-ASP-LYS-CYS-GLU-CYS-VAL-LYS-HIS-NH2, (DISULFIDE BONDS BETWEEN CYS3 AND CYS21/CYS8 AND CYS26/ CYS12 AND CYS28)
[Molecular Formula]

C142H243N45O39S7
[MDL Number]

MFCD00671413
[MOL File]

142948-19-4.mol
[Molecular Weight]

3429.18
Chemical PropertiesBack Directory
[density ]

1.51±0.1 g/cm3(Predicted)
Safety DataBack Directory
[Symbol(GHS) ]


GHS06
[Signal word ]

Danger
[Hazard statements ]

H330-H311-H301
[Precautionary statements ]

P280-P302+P352-P312-P322-P361-P363-P405-P501-P264-P270-P301+P310-P321-P330-P405-P501-P260-P271-P284-P304+P340-P310-P320-P403+P233-P405-P501
Hazard InformationBack Directory
[Uses]

Scyllatoxin (Leiurotoxin I) is a peptide toxin, it can be isolated from the venom of the scorpion (Leiurus quinquestriatus hebraeus). Scyllatoxin is a blocker of small-conductance KCa (SK) channel. Scyllatoxin enhances both norepinephrine (NE) and epinephrine (Epi) release in vivo[1].
[in vivo]

Scyllatoxin (2 μM) increases basal Epi release, the nerve stimulation-induced Epi release and the exogenous acetylcholine (Ach)-induced catecholamine release by microdialysis technique to the left adrenal medulla of anesthetized adult male Wistar rats[2].

[References]

[1] Auguste P, et al. Scyllatoxin, a blocker of Ca(2+)-activated K+ channels: structure-function relationships and brain localization of the binding sites. Biochemistry. 1992 Jan 28;31(3):648-54. DOI:10.1021/bi00118a003
[2] Akiyama T, et al. Role of Ca2+-activated K+ channels in catecholamine release from in vivo rat adrenal medulla. Neurochem Int. 2010 Jan;56(2):263-9. DOI:10.1016/j.neuint.2009.10.010
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