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neo calcium binding protein
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     Calcium and Apoptosis
     Ca~(2+)与细胞凋亡
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     Neo-localization
     通信大鳄的“新本地化”
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     About Calcium
     补钙切莫一“钙”而论
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     On Neo-Terrorism
     试论新恐怖主义
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     Electrocardiogram and measurement of blood calcium were obtained from 57 neo-nates.
     本文对57例新生儿进行了心电图检查及血钙测定。
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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...

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.

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

Both Calmodulin(CaM) and a Neo Calcium Binding Protein(NCBP) were purified from Brassica campestris pollen by phenyl Sepharose CL 4B hydrophobic chromato graphy and DEAE F.F.ion exchange chromatography.Two proteins were shown to be h omogeneous by SDS PAGE, PAGE and IEF.Molecular weights and pI points of pollen CaM and NCBP are 18.8 and 16.3 kD,3.6 and 4.2 respectively. Pollen CaM can activ ate bovine heart cyclic nucleotide phosphodiesterase, pollen NCBP is not notable . Pollen CaM shows Calcium...

Both Calmodulin(CaM) and a Neo Calcium Binding Protein(NCBP) were purified from Brassica campestris pollen by phenyl Sepharose CL 4B hydrophobic chromato graphy and DEAE F.F.ion exchange chromatography.Two proteins were shown to be h omogeneous by SDS PAGE, PAGE and IEF.Molecular weights and pI points of pollen CaM and NCBP are 18.8 and 16.3 kD,3.6 and 4.2 respectively. Pollen CaM can activ ate bovine heart cyclic nucleotide phosphodiesterase, pollen NCBP is not notable . Pollen CaM shows Calcium ion effect in both SDS PAGE and PAGE, while NCBP onl y does in PAGE. The amino acid composition of pollen CaM and NCBP is different, b o th contain more acidic amino acids and a Cys, but lack Trp.Both of their N term inus are blocked and C terminus of pollen CaM is Met Ala Lys COOH.Their pe p tide maps in HPLC and CD spectrums are different. The Cys of pollen CaM was modi f ied by DTNB and the PDE activity by CaM activation is marked descent. From above we can conclude that pollen NCBP is a new Calcium Binding Protein different from pollen CaM.

以油菜花粉(Brasicacampestris)为材料纯化了钙调素(CaM),并得到一种新钙结合蛋白(NCBP)。经SDSPAGE、PAGE和等电聚焦电泳(IEF)鉴定,这两种蛋白质均表现均一。CaM分子量为188kD,NCBP为163kD,等电点分别为36和42。研究证明花粉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(简称PDE)有明显的激活作用,而花粉NCBP不明显。花粉CaM在PAGE和SDSPAGE中电泳行为有Ca2+效应,而NCBP仅表现在PAGE中。经氨基酸组成分析表明两种蛋白质氨基酸组成不同,但均含有较多的酸性氨基酸,不含Trp,含1个Cys。CaM和NCBPN端均为封闭,CaMC端为MetAlaLysCOOH。两种蛋白质具有不同的肽谱和CD谱。用DTNB修饰花粉CaMCys残基,则激活PDE的能力明显下降。

 
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