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Type: Artigo de periódico
Title: Characterization Of A Myotoxin From The Duvernoy's Gland Secretion Of The Xenodontine Colubrid Philodryas Olfersii (green Snake): Effects On Striated Muscle And The Neuromuscular Junction.
Author: Prado-Franceschi, J
Hyslop, S
Cogo, J C
Andrade, A L
Assakura, M T
Reichl, A P
Cruz-Höfling, M A
Rodrigues-Simioni, L
Abstract: A myotoxin has been isolated from the Duvernoy's gland (DG) secretion of the xenodontine colubrid Philodrvas olfersii (green snake) by gel filtration on Sephadex G-100 SF. Under non-reducing and reducing conditions in SDS-PAGE, the myotoxin migrates as a single band with a mol. wt. of 20000. The toxin has 182 amino acid residues (approximately 20% acidic), a pI of 4.8 and a blocked N-terminal. In the chick biventer cervicis preparation, P. olfersii myotoxin partially blocks potassium-evoked contractures without affecting either the twitch-tension resulting from indirect stimulation or the contractures evoked by acetylcholine. Both the DG secretion and the myotoxin increase the serum creatine kinase (CK) levels of mice and stimulate the release of CK from the biventer cervicis preparation in a dose- and time-dependent manner. The varying degrees of muscle cell lysis and extensive widening of the intercellular spaces caused by the DG secretion are reproduced by the myotoxin, with the exception that in the latter the partial or total loss of transverse muscle striations is restricted to the muscle periphery. This myotoxin is the first such protein to be characterized from a DG secretion.
Subject: Acetylcholine
Chromatography, Gel
Creatine Kinase
Crotalid Venoms
Dose-response Relationship, Drug
Electric Stimulation
Electrophoresis, Polyacrylamide Gel
Exocrine Glands
In Vitro Techniques
Muscle Contraction
Neck Muscles
Neuromuscular Junction
Potassium Chloride
Snake Venoms
Species Specificity
Time Factors
Citation: Toxicon : Official Journal Of The International Society On Toxinology. v. 36, n. 10, p. 1407-21, 1998-Oct.
Rights: fechado
Date Issue: 1998
Appears in Collections:Unicamp - Artigos e Outros Documentos

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