The primary structure of ammodytin L, a myotoxic phospholipase A2 homologue from Vipera ammodytes venom.
A new myotoxic phospholipase A2 homologue, having a serine residue in position 49 instead of highly conserved aspartic acid, was found in the venom of Vipera ammodytes. The primary structure revealed additional mutations in the positions important for enzymatic activity. Tyr28 is exchanged for a histidine and Gly33 for asparagine. These changes render earlier-reported weak enzymatic activity unlikely. The role of this rather abundant venom fraction is apparently in myotoxicity, which was confirmed in the muscle-cell culture from neonatal rats. The muscle-cell culture proved to be a good tool to investigate the effects of various myotoxins on muscle cells.
Krizaj
I
I
Department of Biochemistry, J. Stefan Institute, Ljubljana, Slovenia.
Bieber
A L
AL
Ritonja
A
A
Gubensek
F
F
D000595:Amino Acid Sequence; D000818:Animals; D000831:Animals, Newborn; D002459:Cell Fusion / Q000187:drug effects; D002478:Cells, Cultured; D008969:Molecular Sequence Data; D009132:Muscles / Q000166:cytology / Q000187:drug effects / Q000502:physiology; D010741:Phospholipases A / Q000235:genetics*; D054467:Phospholipases A2; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D014757:Viper Venoms / Q000235:genetics* / Q000302:isolation & purification / Q000494:pharmacology
D014757:Viper Venoms; C065419:ammodytin L; D010741:Phospholipases A; D054467:Phospholipases A2