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Titolo:
A new insect neurotoxin AngP(1) with analgesic effect from the scorpion Buthus martensii Karsch: purification and characterization
Autore:
Guan, RJ; Wang, M; Wang, D; Wang, DC;
Indirizzi:
Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China Chinese Acad Sci Beijing Peoples R China 100101 100101, Peoples R China
Titolo Testata:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 1, volume: 58, anno: 2001,
pagine: 27 - 35
SICI:
1397-002X(200107)58:1<27:ANINAW>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANDROCTONUS-AUSTRALIS HECTOR; AMINO-ACID-SEQUENCES; SODIUM-CHANNELS; TOXIN; VENOM; BINDING;
Keywords:
analgesic effect; characterization; purification; scorpion toxin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Wang, DC Chinese Acad Sci, Inst Biophys, 15 Datun Rd,Chaoyang Dist, Beijing 100101,Peoples R China Chinese Acad Sci 15 Datun Rd,Chaoyang Dist Beijing Peoples R China 100101
Citazione:
R.J. Guan et al., "A new insect neurotoxin AngP(1) with analgesic effect from the scorpion Buthus martensii Karsch: purification and characterization", J PEPT RES, 58(1), 2001, pp. 27-35

Abstract

An insect toxin named BmK AngP1 was purified from the venom of the scorpion Buthus martensii Karsch (BmK). It also shows an evident analgesic effect on mice, but is interestingly devoid of mammalian toxicity. Bioassay showedthat the CPU value of AngP1 was 0.01 mug/body (approximate to 30 mg) for the excitatory insect toxicity and 43.0% inhibition efficiency for analgesiaat a dose of 5 mg/kg. However, even at the dosage of 10 mg/kg no detectable toxicity on mice could be found. The isoelectric point (pl) value for AngP1 was 4.0, and its molecular mass analyzed by MALDI-TOF MS was 8141.0. Thefirst 15 N-terminal residues of AngP1 were determined by Edman degradationand showed high similarity to that of other excitatory scorpion insect toxins. The circular dichroism spectroscopy measured on a JASCO J-720 system showed that there were 10.4% alpha -helix, 46.2% beta -strand and 14.1% turnstructure in this peptide. Under two conditions single crystals of AngP1 were obtained.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 15:34:43