Purification and characterization of myotoxin IV, a phospholipase A2variant, fromBothrops aspersnake venom
作者:
Cecilia Diaz,
Bruno Lomonte,
Fernando Zamudio,
José María Gutiérrez,
期刊:
Natural Toxins
(WILEY Available online 1995)
卷期:
Volume 3,
issue 1
页码: 26-31
ISSN:1056-9014
年代: 1995
DOI:10.1002/nt.2620030107
出版商: John Wiley&Sons, Inc.
关键词: Snake venom;Myotoxin;Phospholipases A2;Lys‐49 variant;Myonecrosis
数据来源: WILEY
摘要:
AbstractA basic myotoxic protein was purified fromBothrops asper venom. Like other basicBothropsmyotoxins, myotoxin IV induces acute muscle damage after intramuscular injection in mice and disrupts negatively charged liposomes but not positively charged ones. Furthermore, this protein exerts a weak anticoagulant effect only at concentrations of 40 μg/ml or higher, and is devoid of phospholipase A2activity. Rabbit polyclonal antibodies toB. aspermyotoxin II, a related lysine‐49 isoform, cross‐react strongly with myotoxin IV by enzyme immunoassay, indicating a high degree of antigenic similarity between these two proteins. The fact that both toxins have similar amino acid compositions and amino‐terminal sequences, including leucine‐5 and glutamine‐11, 2 amino acid residues conserved in all lysine‐49 phospholipase A2variants purified, strongly suggests thatB. aspermyotoxin IV is a lysine‐49 phospholipase A2. © 1995
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