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少棘巨蜈蚣（ＳｃｏｌｏｐｅｎｄｒａｓｕｂｓｐｉｎｉｐｅｓｍｕｔｉｌａｎｓＬ．Ｋｏｃｈ）经９５％乙醇脱脂后，再经４℃水冷渗，水提液低温旋转浓缩，冻干，得到的冻干粉先后经过ＳｅｐｈａｄｅｘＧ－２５柱，等电聚焦制备电泳，再经ＳｅｐｈａｄｅｘＧ－１５０柱，ＳｅｐｈａｄｅｘＧ－１００柱，最后经ＨＰＬＣ制备得到一个纯的碱性蛋白，命名为ＳＳｍｐ－ｄ．该蛋白经ＨＰＬＣ、超薄等电聚焦电泳检验是均一的．采用ＨＰＬＣ和Ｐｒｏｔｅｉｎ－ＰａｋＴＭ１２５柱测定其分子量为２４．６４ｋＤ．ＩＥＦ－ＨＰＣＥ显示其等电点为９．２７．氨基酸分析表明ＳＳｍｐ－ｄ含较多的Ａｒｇ、Ｌｙｓ等碱性氨基酸，另外还含有较多的Ａｌａ、Ｌｅｕ．使用蛋白质自动序列分析仪测定了ＳＳｍｐ－ｄＮ端的１１个氨基酸，序列为ＮＨ３＋－Ａｓｐ－Ｖａｌ－Ａｓｎ－Ｐｈｅ－Ａｒｇ－Ｌｅｕ－Ｓｅｒ－Ｇｌｙ－Ａｌａ－Ａｓｐ－Ｐｒｏ．
ScolopendrasubspinipesmutilansL. Koch defatted with 95% ethanol, and then by 4 ℃ water-cooling, the aqueous extract was concentrated by low temperature rotation, lyophilized, the resulting lyophilized powder was SephadexG-25 column, followed by isoelectric focusing electrophoresis , And then by SephadexG-150 column, SephadexG-100 column, finally prepared by HPLC to obtain a pure basic protein, named SSmp-d. The protein by HPLC, ultra-thin isoelectric focusing electrophoresis test is uniform. Its molecular weight was 24.64kD by HPLC and Protein-PakTM125 column. IEF-HPCE shows an isoelectric point of 9.27. Amino acid analysis showed that SSmp-d contains more basic amino acids such as Arg and Lys and more Ala and Leu. The 11 amino acids of the SSmp-dN end were sequenced using a protein automated sequence analyzer and the sequence was NH3 + -Asp-Val-Asn-Phe-Arg-Leu-Ser-Gly-Ala-Asp-Pro.