Kondo K, Toda H, Narita K
J Biochem. 1981 Jan;89(1):37-47. doi: 10.1093/oxfordjournals.jbchem.a133201.
Bungarus multicinctus phospholipase A was reduced and carboxymethylated. The RCM-enzyme was digested with TPCK-trypsin or cleaved with cyanogen bromide followed by chymotrypsin digestion. The resulting peptide mixtures were fractionated by gel filtration on Sephadex G-50 and G-25 columns or by DEAE-cellulose (DE-32) column chromatography. Further purification of the peptide mixtures was performed by paper electrophoresis at pH 3.5 or 6.5 or by paper chromatography. The sequences of isolated peptides were determined by the manual Edman or dansyl-Edman method. From the sequences of these peptides the whole enzyme sequence (total 118 residues) was deduced. The complete sequence of the enzyme is similar to those of phospholipases A2 from other snake venoms and mammalian pancreas. Further, a 58% sequence homology was found between the present phospholipase A and the A chain of beta 1-bungarotoxin, a presynaptic neurotoxin having weak phospholipase A activity, contained in the same venom.
多环扁尾海蛇磷脂酶A被还原并羧甲基化。还原羧甲基化酶（RCM-酶）用TPCK-胰蛋白酶消化或用溴化氰裂解，随后进行糜蛋白酶消化。所得肽混合物通过在Sephadex G-50和G-25柱上进行凝胶过滤或通过DEAE-纤维素（DE-32）柱色谱进行分离。肽混合物的进一步纯化通过在pH 3.5或6.5下进行纸电泳或通过纸色谱进行。分离肽的序列通过手动埃德曼法或丹磺酰-埃德曼法测定。从这些肽的序列推导出整个酶序列（共118个残基）。该酶的完整序列与其他蛇毒和哺乳动物胰腺中的磷脂酶A2的序列相似。此外，在本磷脂酶A与同一毒液中含有的具有弱磷脂酶A活性的突触前神经毒素β1-银环蛇毒素的A链之间发现了58%的序列同源性。
