Nishida S, Terashima M, Tamiya N
Toxicon. 1985;23(1):87-104. doi: 10.1016/0041-0101(85)90112-6.
Two basic phospholipases A2 (Pa-11 and Pa-13) have been isolated from the venom of an Australian elapid snake, Pseudechis australis (king brown snake). The reduced and S-carboxymethylated phospholipases A2 were digested with trypsin and the resulting peptides were purified by a combination of chromatography on a DEAE-cellulose DE-52 column and gel filtration procedures. Eleven main peptides from Pa-11 and 9 peptides from Pa-13 could account for the amino acid compositions of the respective enzyme molecules. The alignment of the tryptic peptides and unelucidated regions of the amino acid sequences of tryptic peptides were established by the analysis of the peptides obtained by chymotryptic and/or Staphylococcal protease digestions. Each phospholipase A2 consisted of a single chain of 118 amino acid residues, including 14 half-cystine residues. Although Pa-11 is enzymatically 30-times as active as Pa-13 and highly toxic as compared to Pa-13, they are highly homologous in their amino acid sequences. They are also homologous to the enzymes from mammalian pancreas and the other snake venom phospholipases A2, especially to those from snakes belonging to the subfamilies Acanthophiinae and Laticaudinae.
从澳大利亚眼镜蛇科蛇(棕伊澳蛇)的毒液中分离出了两种基本的磷脂酶A2(Pa - 11和Pa - 13)。将还原和S - 羧甲基化的磷脂酶A2用胰蛋白酶消化,所得肽段通过在DEAE - 纤维素DE - 52柱上的色谱法和凝胶过滤程序相结合进行纯化。来自Pa - 11的11个主要肽段和来自Pa -