蟾蜍细胞溶素的纯化及其生化特性研究

Purification and Some Properties of Lysin from Bufo Japonicus

利用阴离子交换和凝胶过滤柱层析等方法对蟾蜍卵黄外被细胞溶素进行了分离纯化，获得了高纯度的样品．该酶的质量为３２ｋＤ，其特异性ＭＣＡ－人工合成底物为Ｂｏｃ－Ｇｌｎ－Ａｒｇ－Ａｒｇ－ＭＣＡ，能被ＤＦＰ、ＳＢＴＩ、ｌｅｕｐｅｐｔｉｎ和ｐ－ＡＭＰＳＦ等蛋白酶抑制剂所强烈抑制，但不受ｃｈｙｍｏｓｔａｔｉｎ、ｂｅｓｔａｔｉｎ、Ｅ－６４和ＥＤＴＡ等的影响。

To study its biochemical properties,lysin from Bufo japonicus was purified with anion exchange and gel filtration chromatography.It was found that its mass was 32 kD and its specific MCA substrate was Boc Gln Arg Arg MCA.The purified lysin was strongly inhibited by DFP,SBTI,leupeptin and p AMPSF,but not affected by chymostatin,bestatin,E 64 and EDTA,which indicates that it is a kind of serine type protease.