【摘要】 以赤子爱胜蚓（ＥｉｓｅｎｉａＦｏｅｔｉｄａ）为材料分离纯化了钙调素（Ｃａｌｍｏｄｕｌｉｎ，ＣａＭ），并得到一种新的钙结合蛋白（Ｎｅｏ－ＣａｌｃｉｕｍＢｉｎｄｉｎｇＰｒｏｔｅｉｎ，ＮＣＢＰ）经ＳＤＳ－ＰＡＧＥ、ＰＡＧＥ和等电聚焦电泳鉴定，这两种蛋白均表现均一。ＣａＭ分子量为１８．９ｋＤ，ＮＣＢＰ为１６ｋＤ，等电点分别为３．６和４．３，两种蛋白具有不同的肽谱。研究证明蚯蚓ＣａＭ具有与其他来源ＣａＭ所特有的性质，对环核苷酸磷酸二酯酶有明显的激活作用，电泳行为受Ｃａ２＋的影响出现ＣａＭ特征性电泳行为，ＮＣＢＰ亦有类似性质。ＣａＭ和ＮＣＢＰＮ－端均为Ｇｌｙ，ＣａＭＣ－末端为Ｍｅｔ。经氨基酸组成分析表明蚯蚓ＣａＭ及ＮＣＢＰ和其他动物ＣａＭ一样，不含Ｃｙｓ和Ｔｒｐ。其中Ｐｈｅ／Ｔｙｒ比分别为８∶１和７∶２。可观察到它们的特征性紫外吸收光谱更多还原

【Abstract】 Both Calmodulin(CaM) and a Neo Calcium Binding Protein(NCBP) were separated and purified from earthworm(Eisenia foetida) by phenyl sepharose CL 4B hydrophobic chromatography and DEAE F.F.ion exchange chromatography. Two proteins were shown to be homogeneous by SDS PAGE, PAGE, and IEF. Molecular weight and pI of CaM and NCBP are 18.9 kD and 16kD, 3.6 and 4.3 respectively. Their peptide map is different. Both of thier N terminus are Gly. C terminus of CaM is Met. The electrophoretic mobility of earthworm CaM and NCBP effected by Ca 2+ is similarly as that of the bovine brain CaM. Earthworm CaM can activate bovine heart cyclic nucleotide phosphodiesterase, NCBP has similar properties too. The Phe/Tyr ratio is 8∶1, while that of NCBP is 7∶2. We can observe thier characterstic UV absorption peaks. A Comparison between the properties of earthworm CaM and NCBP indicates that they are similar to each other.更多还原