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-cyclic-nucleotide phosphodiesterase
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     Identification and Characterization of PDE5 cGMP-specific Cyclic Nucleotide Phosphodiesterase
     磷酸二酯酶同工酶PDE5的纯化及性质研究
短句来源
     Determination of calmodulin by cyclic nucleotide phosphodiesterase method
     钙调素的环核苷酸磷酸二酯酶检测法
短句来源
     Progress in selective inhibitors of cyclic nucleotide phosphodiesterase
     选择性磷酸二酯酶抑制剂研究进展
短句来源
     Preparation of Calmodulin Dependent Cyclic Nucleotide Phosphodiesterase
     钙调素依赖性的环核苷酸磷酸二酯酶的制备
短句来源
     CYTOCHEMICAL LOCALIZATION OF 3',5'-CYCLIC NUCLEOTIDE PHOSPHODIESTERASE ACTIVITY WITH ELECTRON MICROSCOPY IN RAT THYROID
     大白鼠甲状腺细胞膜系统3′,5′-环核苷酸磷酸二酯酶活性的电镜细胞化学定位
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Benzylisoquinoline compounds antagonized calmodulin ( CaM ) to inhibit the activity of CaM-dependent cyclic nucleotide phosphodiesterase ( CaM-PDE ) . The anti-CaM ability was relevant to the hydrophobicity of non-polar terminus in the antagonist molecule. The antagonistic potency increased with the increase of hydrophobicity while the anti-CaM ability did not change whether the polar terminus is tertiary amine or quaternary amine. As far as our knowledge goes, compound D3, with IC54 value 2.8 μmol/L,...

Benzylisoquinoline compounds antagonized calmodulin ( CaM ) to inhibit the activity of CaM-dependent cyclic nucleotide phosphodiesterase ( CaM-PDE ) . The anti-CaM ability was relevant to the hydrophobicity of non-polar terminus in the antagonist molecule. The antagonistic potency increased with the increase of hydrophobicity while the anti-CaM ability did not change whether the polar terminus is tertiary amine or quaternary amine. As far as our knowledge goes, compound D3, with IC54 value 2.8 μmol/L, was the most potent CaM antagonist among benzylisoquinoline compounds according to the PDE assay system.

苄基异喹啉类化合物拮抗钙调素(CaM),对环核苷酸磷酸二酯酶(CaM-PDE)产生抑制作用。它们的拮抗能力与分子中非极性端的疏水性相关,增强疏水性能增强拮抗性;极性端为叔胺或季铵离子时,抗CaM性基本不变;在受试的化合物中,D_3的抗CaM活性最强,IC_(50)值为2.8μmol/L。

Localization of 3', 5'-cyclic nucleotide phosphodiesterase activity in thyroid follicular cells and endothelium was examined by cytochemical methods for electron microscopy. In thyroid follicular cells reaction product deposition associated with 3', 5'-cyclic nucleotide phosphodiesterase activity was localized at the plasma membrane. In these cells, the enzyme activity appeared mostly localized on the apical and lateral plasma membrane, and also appeared on the outer surface of nuclear envelope,...

Localization of 3', 5'-cyclic nucleotide phosphodiesterase activity in thyroid follicular cells and endothelium was examined by cytochemical methods for electron microscopy. In thyroid follicular cells reaction product deposition associated with 3', 5'-cyclic nucleotide phosphodiesterase activity was localized at the plasma membrane. In these cells, the enzyme activity appeared mostly localized on the apical and lateral plasma membrane, and also appeared on the outer surface of nuclear envelope, endoplasmic reticulum and Golgi apparatus. However, when cAMP and snake venom were omitted simultaneously, no enzyme activity was observed. 3', 5'-cyclic nucleotide phosphodiesterase activity also appeared on the luminal surface of endothelium of small blood vessels.

本研究用酶电镜细胞化学法观察了大白鼠甲状腺细胞3′,5′-环核苷酸磷酸二酯酶活性的定位。结果证明,3′,5′-环核苷酸磷酸二酯酶的活性定位于甲状腺滤泡细胞的顶部细胞膜和微绒毛,在内质网则存在于膜的外表面,在甲状腺滤泡细胞核也位于核膜的外表面。在甲状腺滤泡上皮细胞之间的微血管内皮细胞膜上也观察到了大量3′,5′-环核苷酸磷酸二酯酶的阳性反应颗粒。

Calmodulin (CaM) was separated from Peking duck brain extract by Phenyl-Sepharose affinity ohromatography and further purified by Sephadex G-50. The purified CaM was shown to be homogeneous by SDS-PAGE and IEF with a molecular weight of 19,000, pI of 4.15, and an extinction coefficient ε2761m 1% of 1.83. The characteristic mobility change of CaM in the presence of Ca2+ was observed.The Ca2+-activition of bovine cyclic nucleotide phosphodiesterase could be enhanced by the addition of CaM. Among 146 amino...

Calmodulin (CaM) was separated from Peking duck brain extract by Phenyl-Sepharose affinity ohromatography and further purified by Sephadex G-50. The purified CaM was shown to be homogeneous by SDS-PAGE and IEF with a molecular weight of 19,000, pI of 4.15, and an extinction coefficient ε2761m 1% of 1.83. The characteristic mobility change of CaM in the presence of Ca2+ was observed.The Ca2+-activition of bovine cyclic nucleotide phosphodiesterase could be enhanced by the addition of CaM. Among 146 amino acid residues, there are 23 aspartic acid, 25 glutamic acid, and no cysteine and tryptophan, the phenylala-nine/tyrosine ratio is high (8:2). Its UV absorption peaks occur at about 252,259, 265, 268.5 and 276nm. The enhancement of fluorescence of CaM could be induced by Ca2+. Some of physical properties of porcine, bovine and duck CaM are compared.

钙调素(Calmodulin,简称CaM)是一种多生理功能的调节蛋白,在脑的功能活动中有重要作用。本文采用苯基琼脂糖(phenyl-Sepharose CL 4B)层析和葡聚糖凝胶(Sephadex G-50)过滤法,从北京鸭脑中分离纯化出CaM。纯化的CaM经SDS-聚丙烯酰胺凝胶电泳(SDS-PAGE)和等电聚焦(IEF)电泳鉴定均为一条区带。分子量为19kD,等电点(pI)为4.15,消光系数为1.83。 对纯化的鸭脑CaM的活性和性质进行了研究。它可明显地激活牛环核苷酸磷酸二酯酶活性,在有Ca~(2+)存在的条件下,SDS-PAGE中出现电泳迁移速度的改变,紫外吸收光谱具有已知CaM特有的吸收多峰形,并观察了Ca~(2+)对荧光发射光谱的影响。其氨基酸组成中,1/3是酸性氨基酸,苯丙氨酸和酪氨酸的比例为8:2。与猪CaM和牛CaM的物理化学性质作了比较。

 
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