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Titolo:
A depressant insect toxin with a novel analgesic effect from scorpion Buthus martensii Karsch
Autore:
Guan, RJ; Wang, CG; Wang, M; 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:
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
fascicolo: 1, volume: 1549, anno: 2001,
pagine: 9 - 18
SICI:
0167-4838(20010910)1549:1<9:ADITWA>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANDROCTONUS-AUSTRALIS HECTOR; ANGSTROM RESOLUTION; CRYSTAL-STRUCTURE; VENOM; NEUROTOXIN; PURIFICATION; SEQUENCE; GENE;
Keywords:
scorpion toxin; depressant insect toxin; analgesic effect; purification; characterization; sequencing;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Wang, DC Chinese Acad Sci, Inst Biophys, 15 Datun Rd, Beijing 100101, Peoples R China Chinese Acad Sci 15 Datun Rd Beijing Peoples R China 100101 hina
Citazione:
R.J. Guan et al., "A depressant insect toxin with a novel analgesic effect from scorpion Buthus martensii Karsch", BBA-PROT ST, 1549(1), 2001, pp. 9-18

Abstract

A new peptide named BmK dITAP3 from scorpion Buthus rnartensii Karsch (BmK) has been identified to possess a dual bioactivity, a depressant neurotoxicity on insects and an analgesic effect on mice. The bioassays also showed that the peptide was definitely devoid of the neurotoxicity on mammals, which indicated that the analgesic effect of BmK dITAP3 could not be ascribed to the syndromic effects of a mammalian neurotoxicity. BmK dITAP3 exhibited43.0% inhibition efficiency of the analgesic effect on mice at a dose of 5mg/kg and the FPU value of 0.5 mug/body (similar to 30 mg) on the fly larvae. The pI value and the molecular mass determined by MALDI-TOF MS for dITAP3 were 6.5 and 6722.7, respectively. Its first 15 N-terminal residues weredetermined by Edman degradation, based on which the full amino acid sequence was deduced from the cDNA sequence encoding the peptide with 3 ' -RACE. Circular dichroism and sequence based prediction analyses showed dITAP3 mayhave a similar molecular scaffold as the most scorpion toxins but with features of the more beta structures and much less of alpha helix. The detailsof the purification, characterization and sequencing as well as the sequence comparison with other depressant insect toxins and the correlation between the analgesic effect and the insect toxicity will be reported and discussed. respectively. (C) 2001 Elsevier Science BN. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 00:59:51