海葵毒素多肽的分离和初步表征  

Isolation and Characterization of Toxin Polypeptides from Sea Anemone Actinia cari

作　　者：禚如朋[1] 付宏征[1] 仲崇波[2] 王晓良[2] 林文翰[1] 张礼和[1] 

机构地区：[1]北京大学医学部天然药物及仿生药物国家重点实验室,北京1000832 [2]中国医学科学院药物研究所,北京100050

出　　处：《生物化学与生物物理进展》2001年第4期514-518,共5页Progress In Biochemistry and Biophysics

摘　　要：经冻融法提取 ,丙酮沉淀 ,SPSephadexC 2 5强离子交换和HPLCODSC18反相色谱层析 ,从海葵Actiniacari中提纯到两个新的毒素多肽 ,命名为RSAPⅠ和RSAPⅡ ,经SDS 聚丙烯酰胺凝胶电泳 (SDS PAGE)和基质辅助激光解吸电离飞行时间质谱 (MALDI TOF MS)鉴定RSAPⅠ和RSAPⅡ均为单一成分 ,相对分子质量分别为 5 0 0 8和 4992 .初步钠通道药理学实验表明 ,RSAPⅠ和RSAPⅡ对豚鼠心室肌细胞钠通道表现出活性 ,RSAPⅠ使钠离子内流增加 ,起开放作用 ;RSAPⅡ使钠离子内流减少 ,起阻滞作用 .二者的圆二色谱均表现为10 0 %Two toxin polypeptides (designated RSAP I and RSAP II) have been isolated from Sea anemone Actinia cari. Toxins isolation was accomplished by freezing-thawing extraction, acetone fractional precipitation, cation exchange chromagraphy on SP Sephadex C 25 and reverse phase HPLC on ODS C-18. They were found to be homogenous by SDS-PAGE and MALDI-TOF-MS, and their relative molecular masses are 5 008 and 4 992, respectively. They are found to be active on sodium channel in Guinea pig cardiac cell, RSAPI, increasing inward Na (+) currents, opens the sodium channel; RSAP It, decreasing inward Na ( +) currents, inhibits the opening of the sodium channel. The circular dichroic spectra of these two polypeptides are 100% beta turn.

关 键 词：海葵 海葵毒素 分离纯化 

分 类 号：R996.3[医药卫生—毒理学] R282.77[医药卫生—药学]