Author/Editor | Ritonja, A; Machleidt, W; Turk, V; Gubenšek, F | |
Title | Amino-acid sequence of ammodytoxin B partially reveals the location of the site of toxicity of ammodytoxins | |
Type | članek | |
Source | Biol Chem Hoppe Seyler | |
Vol. and No. | Letnik 367, št. 9 | |
Publication year | 1986 | |
Volume | str. 919-23 | |
Language | eng | |
Abstract | The complete amino-acid sequence of ammodytoxin B, a presynaptically toxic phospholipase A2 isolated from Vipera ammodytes ammodytes venom, was determined by manual and automated protein sequencing. Ammodytoxin B (i.v. LD50 = 0.58 mg/kg for white mice) is 30-fold less toxic than ammodytoxin A, the most toxic phospholipase isolated from the same venom. The two proteins (each 122 residues long) differ in only 3 residues located in positions 115, 118 and 119 (numbering according to R. Renetseder et al. (1985) J. Biol. Chem. 260, 11627-11634) suggesting that an exposed hydrophobic residue in position 115 and a basic residue in position 118 may be responsible for the increased toxicity of ammodytoxin A and should form at least one part of the site of toxicity in ammodytoxins. | |
Descriptors | PHOSPHOLIPASES PHOSPHOLIPASES A VIPER VENOMS AMINO ACID SEQUENCE CATTLE CYANOGEN BROMIDE MICE PEPTIDE FRAGMENTS STRUCTURE-ACTIVITY RELATIONSHIP VIPER VENOMS |